A pseudoknotted tRNA variant is a substrate for tRNA (cytosine-5)-methyltransferase from Xenopus laevis
Identifieur interne : 000541 ( Istex/Corpus ); précédent : 000540; suivant : 000542A pseudoknotted tRNA variant is a substrate for tRNA (cytosine-5)-methyltransferase from Xenopus laevis
Auteurs : Hervé Brulé ; Henri Grosjean ; Richard Giegé ; Catherine FlorentzSource :
- Biochimie [ 0300-9084 ] ; 1998.
English descriptors
- KwdEn :
- Teeft :
- Acceptor, Acceptor branch, Anticodon, Biochimie, Canonical, Canonical trnas, Coli, Denaturing polyacrylamide, Elution solution, Enzymatic formation, Enzyme, Eukaryotic trna, Gieg6, Grosjean, Laevis, Methylation, Microinjected, Modification, Modification pattern, Mosaic, Mosaic virus, Nuclease, Nucleic, Nucleic acids, Nucleotide, Oocyte, Potential target nucleotides, Press washington, Rna, Rnase, Structural features, Transcript, Trna, Turnip, Tymv, Tymv domain, Tymv structure, Viral, Xenopus, Xenopus laevis, Xenopus laevis oocyte, Xenopus laevis oocytes, Xenopus oocytes, Yeast, Yeast trna, Yeast trnas.
Abstract
Abstract: tRNA post-transcriptional modification enzymes of Xenopus laevis were proposed previously to belong to two major groups according to their sensitivity to structural perturbations in their substrates. To further investigate the structural variations tolerated by these enzymes, the tRNA-like domain of turnip yellow mosaic virus RNA (88 nucleotides in length) has been microinjected into the oocytes of Xenopus laevis. This RNA possesses 12 potential target nucleotides for modification within a structure including a pseudoknotted folding, an extended anticodon stem, and unusual D-loop/T-loop interactions. Results indicate that only cytosine-42, a position equivalent to C-49 in canonical tRNAs, was quantitatively modified into m5C in the microinjected RNA. Modification was detected to high levels, indicating that at least one enzyme tolerates non-canonical structural features.
Url:
DOI: 10.1016/S0300-9084(99)80003-0
Links to Exploration step
ISTEX:02400B0AE40FC063AB70C507AC2E17A605294A4DLe document en format XML
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trna</term><term>Gieg6</term><term>Grosjean</term><term>Laevis</term><term>Methylation</term><term>Microinjected</term><term>Modification</term><term>Modification pattern</term><term>Mosaic</term><term>Mosaic virus</term><term>Nuclease</term><term>Nucleic</term><term>Nucleic acids</term><term>Nucleotide</term><term>Oocyte</term><term>Potential target nucleotides</term><term>Press washington</term><term>Rna</term><term>Rnase</term><term>Structural features</term><term>Transcript</term><term>Trna</term><term>Turnip</term><term>Tymv</term><term>Tymv domain</term><term>Tymv structure</term><term>Viral</term><term>Xenopus</term><term>Xenopus laevis</term><term>Xenopus laevis oocyte</term><term>Xenopus laevis oocytes</term><term>Xenopus oocytes</term><term>Yeast</term><term>Yeast trna</term><term>Yeast trnas</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: tRNA post-transcriptional modification enzymes of Xenopus laevis were proposed previously to belong to two major groups according to their sensitivity to structural perturbations in their substrates. To further investigate the structural variations tolerated by these enzymes, the tRNA-like domain of turnip yellow mosaic virus RNA (88 nucleotides in length) has been microinjected into the oocytes of Xenopus laevis. This RNA possesses 12 potential target nucleotides for modification within a structure including a pseudoknotted folding, an extended anticodon stem, and unusual D-loop/T-loop interactions. Results indicate that only cytosine-42, a position equivalent to C-49 in canonical tRNAs, was quantitatively modified into m5C in the microinjected RNA. 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To further investigate the structural variations tolerated by these enzymes, the tRNA-like domain of turnip yellow mosaic virus RNA (88 nucleotides in length) has been microinjected into the oocytes of Xenopus laevis. This RNA possesses 12 potential target nucleotides for modification within a structure including a pseudoknotted folding, an extended anticodon stem, and unusual D-loop/T-loop interactions. Results indicate that only cytosine-42, a position equivalent to C-49 in canonical tRNAs, was quantitatively modified into m5C in the microinjected RNA. Modification was detected to high levels, indicating that at least one enzyme tolerates non-canonical structural features.</abstract><pmid><json:string>9924976</json:string></pmid><serie><title>FEBS Proc. Meet.</title><language><json:string>unknown</json:string></language><volume>39</volume><pages><first>121</first><last>131</last></pages></serie><copyrightDate>1998</copyrightDate><doi><json:string>10.1016/S0300-9084(99)80003-0</json:string></doi><id>02400B0AE40FC063AB70C507AC2E17A605294A4D</id><score>1</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-8WH36MQS-D/fulltext.pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-8WH36MQS-D/bundle.zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/ark:/67375/6H6-8WH36MQS-D/fulltext.tei"><teiHeader><fileDesc><titleStmt><title level="a" type="main" xml:lang="en">A pseudoknotted tRNA variant is a substrate for tRNA (cytosine-5)-methyltransferase from Xenopus laevis</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher scheme="https://scientific-publisher.data.istex.fr">ELSEVIER</publisher><availability><licence><p>©1998 Société française de biochimie et biologie moléculaire/ Elsevier, Paris</p></licence><p scheme="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M">elsevier</p></availability><date>1998</date></publicationStmt><notesStmt><note type="research-article" scheme="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</note><note type="journal" scheme="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a" type="main" xml:lang="en">A pseudoknotted tRNA variant is a substrate for tRNA (cytosine-5)-methyltransferase from Xenopus laevis</title><author xml:id="author-0000"><persName><forename type="first">Hervé</forename><surname>Brulé</surname></persName><affiliation>UPR 9002 du CNRS, Institut de Biologie Moléculaire et Cellulaire, 15, rue René-Descartes, 67084 Strasbourg cedex, France</affiliation></author><author xml:id="author-0001"><persName><forename type="first">Henri</forename><surname>Grosjean</surname></persName><affiliation>Laboratoire d'Enzymologie et Biochimie Structurales du CNRS, 1, avenue de la Terrasse, 91198 Gif-Sur-Yvette, France</affiliation></author><author xml:id="author-0002"><persName><forename type="first">Richard</forename><surname>Giegé</surname></persName><affiliation>UPR 9002 du CNRS, Institut de Biologie Moléculaire et Cellulaire, 15, rue René-Descartes, 67084 Strasbourg cedex, France</affiliation></author><author xml:id="author-0003"><persName><forename type="first">Catherine</forename><surname>Florentz</surname></persName><affiliation>UPR 9002 du CNRS, Institut de Biologie Moléculaire et Cellulaire, 15, rue René-Descartes, 67084 Strasbourg cedex, France</affiliation><affiliation>Correspondence and reprints</affiliation></author><idno type="istex">02400B0AE40FC063AB70C507AC2E17A605294A4D</idno><idno type="ark">ark:/67375/6H6-8WH36MQS-D</idno><idno type="DOI">10.1016/S0300-9084(99)80003-0</idno><idno type="PII">S0300-9084(99)80003-0</idno><idno type="article-id">99800030</idno></analytic><monogr><title level="j">Biochimie</title><title level="j" type="abbrev">BIOCHI</title><idno type="pISSN">0300-9084</idno><idno type="PII">S0300-9084(00)X0194-0</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1998"></date><biblScope unit="volume">80</biblScope><biblScope unit="issue">12</biblScope><biblScope unit="page" from="977">977</biblScope><biblScope unit="page" to="985">985</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1998</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Abstract: tRNA post-transcriptional modification enzymes of Xenopus laevis were proposed previously to belong to two major groups according to their sensitivity to structural perturbations in their substrates. To further investigate the structural variations tolerated by these enzymes, the tRNA-like domain of turnip yellow mosaic virus RNA (88 nucleotides in length) has been microinjected into the oocytes of Xenopus laevis. This RNA possesses 12 potential target nucleotides for modification within a structure including a pseudoknotted folding, an extended anticodon stem, and unusual D-loop/T-loop interactions. Results indicate that only cytosine-42, a position equivalent to C-49 in canonical tRNAs, was quantitatively modified into m5C in the microinjected RNA. Modification was detected to high levels, indicating that at least one enzyme tolerates non-canonical structural features.</p></abstract><textClass xml:lang="en"><keywords scheme="keyword"><list><item><term>tRNA</term></item><item><term>post-transcriptional modification</term></item><item><term>turnip yellow mosaic virus</term></item><item><term>methylase</term></item><item><term>tertiary structure</term></item><item><term>Xenopus laevis</term></item></list></keywords></textClass><textClass xml:lang="en"><keywords scheme="keyword"><list><head>Abbreviations</head><item><term>TYMV</term><term>turnip yellow mosaic virus</term></item><item><term>TLC</term><term>thin layer chromatography</term></item><item><term>cps</term><term>counts per second</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1998">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-8WH36MQS-D/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier doc found" wicri:toSee="Elsevier, no converted or simple article"><istex:xmlDeclaration>version="1.0" encoding="utf-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//ES//DTD journal article DTD version 5.0.1//EN//XML" URI="art501.dtd" name="istex:docType"></istex:docType><istex:document><article version="5.0" xml:lang="en" docsubtype="fla"><item-info><jid>BIOCHI</jid><aid>99800030</aid><ce:pii>S0300-9084(99)80003-0</ce:pii><ce:doi>10.1016/S0300-9084(99)80003-0</ce:doi><ce:copyright type="unknown" year="1998">Société française de biochimie et biologie moléculaire/ Elsevier, Paris</ce:copyright></item-info><head><ce:title>A pseudoknotted tRNA variant is a substrate for tRNA (cytosine-5)-methyltransferase from <ce:italic>Xenopus laevis</ce:italic></ce:title><ce:author-group><ce:author><ce:given-name>Hervé</ce:given-name><ce:surname>Brulé</ce:surname><ce:cross-ref refid="aff1"><ce:sup>a</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Henri</ce:given-name><ce:surname>Grosjean</ce:surname><ce:cross-ref refid="aff2"><ce:sup>b</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Richard</ce:given-name><ce:surname>Giegé</ce:surname><ce:cross-ref refid="aff1"><ce:sup>a</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Catherine</ce:given-name><ce:surname>Florentz</ce:surname><ce:cross-ref refid="aff1"><ce:sup>a</ce:sup></ce:cross-ref><ce:cross-ref refid="cor1"><ce:sup>*</ce:sup></ce:cross-ref></ce:author><ce:affiliation id="aff1"><ce:label>a</ce:label><ce:textfn>UPR 9002 du CNRS, Institut de Biologie Moléculaire et Cellulaire, 15, rue René-Descartes, 67084 Strasbourg cedex, France</ce:textfn></ce:affiliation><ce:affiliation id="aff2"><ce:label>b</ce:label><ce:textfn>Laboratoire d'Enzymologie et Biochimie Structurales du CNRS, 1, avenue de la Terrasse, 91198 Gif-Sur-Yvette, France</ce:textfn></ce:affiliation><ce:correspondence id="cor1"><ce:label>*</ce:label><ce:text>Correspondence and reprints</ce:text></ce:correspondence></ce:author-group><ce:date-received day="20" month="4" year="1998"></ce:date-received><ce:date-accepted day="5" month="10" year="1998"></ce:date-accepted><ce:abstract id="ab1" class="author" xml:lang="en"><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>tRNA post-transcriptional modification enzymes of <ce:italic>Xenopus laevis</ce:italic> were proposed previously to belong to two major groups according to their sensitivity to structural perturbations in their substrates. To further investigate the structural variations tolerated by these enzymes, the tRNA-like domain of turnip yellow mosaic virus RNA (88 nucleotides in length) has been microinjected into the oocytes of <ce:italic>Xenopus laevis</ce:italic>. This RNA possesses 12 potential target nucleotides for modification within a structure including a pseudoknotted folding, an extended anticodon stem, and unusual D-loop/T-loop interactions. Results indicate that only cytosine-42, a position equivalent to C-49 in canonical tRNAs, was quantitatively modified into m<ce:sup loc="post">5</ce:sup>C in the microinjected RNA. Modification was detected to high levels, indicating that at least one enzyme tolerates non-canonical structural features.</ce:simple-para></ce:abstract-sec></ce:abstract><ce:keywords class="keyword" xml:lang="en"><ce:keyword><ce:text>tRNA</ce:text></ce:keyword><ce:keyword><ce:text>post-transcriptional modification</ce:text></ce:keyword><ce:keyword><ce:text>turnip yellow mosaic virus</ce:text></ce:keyword><ce:keyword><ce:text>methylase</ce:text></ce:keyword><ce:keyword><ce:text>tertiary structure</ce:text></ce:keyword><ce:keyword><ce:text><ce:italic>Xenopus laevis</ce:italic></ce:text></ce:keyword></ce:keywords><ce:keywords class="abr" xml:lang="en"><ce:section-title>Abbreviations</ce:section-title><ce:keyword><ce:text>TYMV</ce:text><ce:keyword><ce:text>turnip yellow mosaic virus</ce:text></ce:keyword></ce:keyword><ce:keyword><ce:text>TLC</ce:text><ce:keyword><ce:text>thin layer chromatography</ce:text></ce:keyword></ce:keyword><ce:keyword><ce:text>cps</ce:text><ce:keyword><ce:text>counts per second</ce:text></ce:keyword></ce:keyword></ce:keywords></head><tail><ce:bibliography><ce:section-title>References</ce:section-title><ce:bibliography-sec><ce:bib-reference id="bib1"><ce:label>[1]</ce:label><sb:reference><sb:contribution langtype="en"><sb:authors><sb:author><ce:surname>Limbach</ce:surname><ce:given-name>P.A.</ce:given-name></sb:author><sb:author><ce:surname>Crain</ce:surname><ce:given-name>P.F.</ce:given-name></sb:author><sb:author><ce:surname>MacCloskey</ce:surname><ce:given-name>J.A.</ce:given-name></sb:author></sb:authors><sb:title><sb:maintitle>Summary: The modified nucleosides of RNA</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Nucleic Acids Res.</sb:maintitle></sb:title><sb:volume-nr>22</sb:volume-nr></sb:series><sb:date>1994</sb:date></sb:issue><sb:pages><sb:first-page>2183</sb:first-page><sb:last-page>2196</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib2"><ce:label>[2]</ce:label><sb:reference><sb:contribution langtype="en"><sb:authors><sb:author><ce:surname>Crain</ce:surname><ce:given-name>P.F.</ce:given-name></sb:author><sb:author><ce:surname>McCloskey</ce:surname><ce:given-name>J.A.</ce:given-name></sb:author></sb:authors><sb:title><sb:maintitle>The RNA modification database</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Nucleic Acids Res.</sb:maintitle></sb:title><sb:volume-nr>25</sb:volume-nr></sb:series><sb:date>1997</sb:date></sb:issue><sb:pages><sb:first-page>126</sb:first-page><sb:last-page>127</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib3"><ce:label>[3]</ce:label><sb:reference><sb:contribution langtype="en"><sb:authors><sb:author><ce:surname>Auffinger</ce:surname><ce:given-name>P.</ce:given-name></sb:author><sb:author><ce:surname>Westhof</ce:surname><ce:given-name>E.</ce:given-name></sb:author></sb:authors><sb:title><sb:maintitle>Appendix 5: location and distribution of modified nucleotides in tRNA</sb:maintitle></sb:title></sb:contribution><sb:host><sb:edited-book><sb:editors><sb:editor><ce:surname>Grosjean</ce:surname><ce:given-name>H.</ce:given-name></sb:editor><sb:editor><ce:surname>Benne</ce:surname><ce:given-name>R.</ce:given-name></sb:editor></sb:editors><sb:title><sb:maintitle>Modification and Editing of RNA</sb:maintitle></sb:title><sb:date>1998</sb:date><sb:publisher><sb:name>ASM Press</sb:name><sb:location>Chichester</sb:location></sb:publisher></sb:edited-book><sb:pages><sb:first-page>569</sb:first-page><sb:last-page>577</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib4"><ce:label>[4]</ce:label><sb:reference><sb:contribution langtype="en"><sb:authors><sb:author><ce:surname>Garcia</ce:surname><ce:given-name>G.A.</ce:given-name></sb:author><sb:author><ce:surname>Goodenough-Lashua</ce:surname><ce:given-name>D.M.</ce:given-name></sb:author></sb:authors><sb:title><sb:maintitle>Mechanisms of RNA modifying and editing enzymes</sb:maintitle></sb:title></sb:contribution><sb:host><sb:edited-book><sb:editors><sb:editor><ce:surname>Grosjean</ce:surname><ce:given-name>H.</ce:given-name></sb:editor><sb:editor><ce:surname>Benne</ce:surname><ce:given-name>R.</ce:given-name></sb:editor></sb:editors><sb:title><sb:maintitle>Modification and Editing of RNA</sb:maintitle></sb:title><sb:date>1998</sb:date><sb:publisher><sb:name>ASM Press</sb:name><sb:location>Washington, D.C.</sb:location></sb:publisher></sb:edited-book><sb:pages><sb:first-page>131</sb:first-page><sb:last-page>168</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib5"><ce:label>[5]</ce:label><sb:reference><sb:contribution langtype="en"><sb:authors><sb:author><ce:surname>Holmes</ce:surname><ce:given-name>W.M.</ce:given-name></sb:author><sb:author><ce:surname>Andraos-Selim</ce:surname><ce:given-name>C.</ce:given-name></sb:author><sb:author><ce:surname>Roberts</ce:surname><ce:given-name>I.</ce:given-name></sb:author><sb:author><ce:surname>Wahab</ce:surname><ce:given-name>S.Z.</ce:given-name></sb:author></sb:authors><sb:title><sb:maintitle>Structural requirements for tRNA methylation</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:title><sb:maintitle>Action of <ce:italic>Escherichia coli</ce:italic> tRNA (guanosine-1) methyltransferase on tRNALeul structural variants</sb:maintitle></sb:title><sb:series><sb:title><sb:maintitle>J. Biol. Chem.</sb:maintitle></sb:title><sb:volume-nr>267</sb:volume-nr></sb:series><sb:date>1992</sb:date></sb:issue><sb:pages><sb:first-page>13440</sb:first-page><sb:last-page>13445</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib6"><ce:label>[6]</ce:label><sb:reference><sb:contribution langtype="en"><sb:authors><sb:author><ce:surname>Redlak</ce:surname><ce:given-name>M.</ce:given-name></sb:author><sb:author><ce:surname>Andraos-Selim</ce:surname><ce:given-name>C.</ce:given-name></sb:author><sb:author><ce:surname>Giegé</ce:surname><ce:given-name>R.</ce:given-name></sb:author><sb:author><ce:surname>Florentz</ce:surname><ce:given-name>C.</ce:given-name></sb:author><sb:author><ce:surname>Holmes</ce:surname><ce:given-name>W.M.</ce:given-name></sb:author></sb:authors><sb:title><sb:maintitle>Interaction of tRNA with tRNA(guanosinel)methyltransferase: binding specificity determinants involve the dinucleotide G36pG37 and tertiary structure</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Biochemistry</sb:maintitle></sb:title><sb:volume-nr>36</sb:volume-nr></sb:series><sb:date>1997</sb:date></sb:issue><sb:pages><sb:first-page>8699</sb:first-page><sb:last-page>8709</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib7"><ce:label>[7]</ce:label><sb:reference><sb:contribution langtype="en"><sb:authors><sb:author><ce:surname>Achsel</ce:surname><ce:given-name>T.</ce:given-name></sb:author><sb:author><ce:surname>Gross</ce:surname><ce:given-name>H.J.</ce:given-name></sb:author></sb:authors><sb:title><sb:maintitle>Identity determinants of human tRNA<ce:sup loc="post">Ser</ce:sup>: Sequence elements necessary for serylation and maturation of a tRNA with a long extra arm</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>EMBO J.</sb:maintitle></sb:title><sb:volume-nr>12</sb:volume-nr></sb:series><sb:date>1993</sb:date></sb:issue><sb:pages><sb:first-page>3333</sb:first-page><sb:last-page>3338</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib8"><ce:label>[8]</ce:label><sb:reference><sb:contribution langtype="en"><sb:authors><sb:author><ce:surname>Auxilien</ce:surname><ce:given-name>S.</ce:given-name></sb:author><sb:author><ce:surname>Crain</ce:surname><ce:given-name>P.F.</ce:given-name></sb:author><sb:author><ce:surname>Trewyn</ce:surname><ce:given-name>R.W.</ce:given-name></sb:author><sb:author><ce:surname>Grosjean</ce:surname><ce:given-name>H.</ce:given-name></sb:author></sb:authors><sb:title><sb:maintitle>Mechanism, specificity and general properties of the yeast enzyme catalysing the formation of inosine 34 in the anticodon of transfer RNA</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>J. Mol. Biol.</sb:maintitle></sb:title><sb:volume-nr>262</sb:volume-nr></sb:series><sb:date>1996</sb:date></sb:issue><sb:pages><sb:first-page>437</sb:first-page><sb:last-page>458</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib9"><ce:label>[9]</ce:label><sb:reference><sb:contribution langtype="en"><sb:authors><sb:author><ce:surname>Edqvist</ce:surname><ce:given-name>J.</ce:given-name></sb:author><sb:author><ce:surname>Grosjean</ce:surname><ce:given-name>H.</ce:given-name></sb:author><sb:author><ce:surname>Straby</ce:surname><ce:given-name>K.</ce:given-name></sb:author></sb:authors><sb:title><sb:maintitle>Identity elements for N2-dimethylation of guanosine-26 in yeast tRNAs</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Nucleic Acids Res.</sb:maintitle></sb:title><sb:volume-nr>20</sb:volume-nr></sb:series><sb:date>1992</sb:date></sb:issue><sb:pages><sb:first-page>6575</sb:first-page><sb:last-page>6581</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib10"><ce:label>[10]</ce:label><sb:reference><sb:contribution langtype="en"><sb:authors><sb:author><ce:surname>Edqvist</ce:surname><ce:given-name>J.</ce:given-name></sb:author><sb:author><ce:surname>Bloomqvist</ce:surname><ce:given-name>K.</ce:given-name></sb:author><sb:author><ce:surname>Straby</ce:surname><ce:given-name>K.B.</ce:given-name></sb:author></sb:authors><sb:title><sb:maintitle>Structural elements in yeast tRNAs required for homologous modification of guanosine-26 into dimethylguanosine-26 by the yeast Trml tRNAmodifying enzyme</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Biochemistry</sb:maintitle></sb:title><sb:volume-nr>33</sb:volume-nr></sb:series><sb:date>1994</sb:date></sb:issue><sb:pages><sb:first-page>9546</sb:first-page><sb:last-page>9551</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib11"><ce:label>[11]</ce:label><sb:reference><sb:contribution langtype="en"><sb:authors><sb:author><ce:surname>Edqvist</ce:surname><ce:given-name>J.</ce:given-name></sb:author><sb:author><ce:surname>Straby</ce:surname><ce:given-name>K.</ce:given-name></sb:author><sb:author><ce:surname>Grosjean</ce:surname><ce:given-name>H.</ce:given-name></sb:author></sb:authors><sb:title><sb:maintitle>Enzymatic formation of N<ce:sup loc="post">2</ce:sup>, N<ce:sup loc="post">2</ce:sup>-dimethylguanosine in eukaryotic tRNA: importance of the tRNA architecture</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Biochimie</sb:maintitle></sb:title><sb:volume-nr>77</sb:volume-nr></sb:series><sb:date>1995</sb:date></sb:issue><sb:pages><sb:first-page>54</sb:first-page><sb:last-page>61</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib12"><ce:label>[12]</ce:label><sb:reference><sb:contribution langtype="en"><sb:authors><sb:author><ce:surname>Wildenauer</ce:surname><ce:given-name>D.</ce:given-name></sb:author><sb:author><ce:surname>Gross</ce:surname><ce:given-name>H.J.</ce:given-name></sb:author><sb:author><ce:surname>Riesner</ce:surname><ce:given-name>D.</ce:given-name></sb:author></sb:authors><sb:title><sb:maintitle>Enzymatic methylation: III. Cadaverine-induced conformational changes in <ce:italic>E coli</ce:italic> tRNA<ce:inf loc="post">f</ce:inf><ce:sup loc="post">Met</ce:sup> as evidenced by the availability of a specific adenosine and a specific cytosine residue for methylation</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Nucleic Acids Res.</sb:maintitle></sb:title><sb:volume-nr>1</sb:volume-nr></sb:series><sb:date>1974</sb:date></sb:issue><sb:pages><sb:first-page>1165</sb:first-page><sb:last-page>1175</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib13"><ce:label>[13]</ce:label><sb:reference><sb:contribution langtype="en"><sb:authors><sb:author><ce:surname>Hori</ce:surname><ce:given-name>H.</ce:given-name></sb:author><sb:author><ce:surname>Saneyoshi</ce:surname><ce:given-name>M.</ce:given-name></sb:author><sb:author><ce:surname>Kumagai</ce:surname><ce:given-name>I.</ce:given-name></sb:author><sb:author><ce:surname>Miura</ce:surname><ce:given-name>K.I.</ce:given-name></sb:author><sb:author><ce:surname>Watanabe</ce:surname><ce:given-name>K.</ce:given-name></sb:author></sb:authors><sb:title><sb:maintitle>Effects of modifications of 4-thiouridine in <ce:italic>E. coli</ce:italic> tRNA<ce:sup loc="post">Met</ce:sup> on its methyl acceptor activity by thermostable Gm-methylases</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>J. Biochem.</sb:maintitle></sb:title><sb:volume-nr>106</sb:volume-nr></sb:series><sb:date>1989</sb:date></sb:issue><sb:pages><sb:first-page>798</sb:first-page><sb:last-page>802</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib14"><ce:label>[14]</ce:label><sb:reference><sb:contribution langtype="en"><sb:authors><sb:author><ce:surname>Kealey</ce:surname><ce:given-name>J.T.</ce:given-name></sb:author><sb:author><ce:surname>Santi</ce:surname><ce:given-name>D.V.</ce:given-name></sb:author></sb:authors><sb:title><sb:maintitle>Stereochemistry of the (m<ce:sup loc="post">5</ce:sup>U54)-methyl transferase catalysis: <ce:sup loc="post">19</ce:sup>F NMR spectroscopy of an enzyme-FUraRNA covalent complex</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Biochemistry</sb:maintitle></sb:title><sb:volume-nr>34</sb:volume-nr></sb:series><sb:date>1995</sb:date></sb:issue><sb:pages><sb:first-page>2441</sb:first-page><sb:last-page>2446</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib15"><ce:label>[15]</ce:label><sb:reference><sb:contribution langtype="en"><sb:authors><sb:author><ce:surname>Gu</ce:surname><ce:given-name>X.</ce:given-name></sb:author><sb:author><ce:surname>Yu</ce:surname><ce:given-name>M.</ce:given-name></sb:author><sb:author><ce:surname>Ivanetich</ce:surname><ce:given-name>K.M.</ce:given-name></sb:author><sb:author><ce:surname>Santi</ce:surname><ce:given-name>D.V.</ce:given-name></sb:author></sb:authors><sb:title><sb:maintitle>Molecular recognition of tRNA by tRNA pseudouridine-55 synthase</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Biochemistry</sb:maintitle></sb:title><sb:volume-nr>37</sb:volume-nr></sb:series><sb:date>1998</sb:date></sb:issue><sb:pages><sb:first-page>339</sb:first-page><sb:last-page>343</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib16"><ce:label>[16]</ce:label><sb:reference><sb:contribution langtype="en"><sb:authors><sb:author><ce:surname>Becker</ce:surname><ce:given-name>H.F.</ce:given-name></sb:author><sb:author><ce:surname>Motorin</ce:surname><ce:given-name>Y.</ce:given-name></sb:author><sb:author><ce:surname>Sissler</ce:surname><ce:given-name>M.</ce:given-name></sb:author><sb:author><ce:surname>Florentz</ce:surname><ce:given-name>C.</ce:given-name></sb:author><sb:author><ce:surname>Grosjean</ce:surname><ce:given-name>H.</ce:given-name></sb:author></sb:authors><sb:title><sb:maintitle>Major identity determinants for enzymatic formation of ribothymidine and pseudouridine in the T-loop of yeast tRNAs</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>J. Mol. Biol.</sb:maintitle></sb:title><sb:volume-nr>274</sb:volume-nr></sb:series><sb:date>1997</sb:date></sb:issue><sb:pages><sb:first-page>505</sb:first-page><sb:last-page>518</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib17"><ce:label>[17]</ce:label><sb:reference><sb:contribution langtype="en"><sb:authors><sb:author><ce:surname>Grosjean</ce:surname><ce:given-name>H.</ce:given-name></sb:author><sb:author><ce:surname>Edqvist</ce:surname><ce:given-name>J.</ce:given-name></sb:author><sb:author><ce:surname>Straby</ce:surname><ce:given-name>K.</ce:given-name></sb:author><sb:author><ce:surname>Giegé</ce:surname><ce:given-name>R.</ce:given-name></sb:author></sb:authors><sb:title><sb:maintitle>Enzymatic formation of modified nucleosides in tRNA: Dependence on tRNA architecture</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>J. Mol. Biol.</sb:maintitle></sb:title><sb:volume-nr>255</sb:volume-nr></sb:series><sb:date>1996</sb:date></sb:issue><sb:pages><sb:first-page>67</sb:first-page><sb:last-page>85</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib18"><ce:label>[18]</ce:label><sb:reference><sb:contribution langtype="en"><sb:authors><sb:author><ce:surname>Giegé</ce:surname><ce:given-name>R.</ce:given-name></sb:author><sb:author><ce:surname>Florentz</ce:surname><ce:given-name>C.</ce:given-name></sb:author><sb:author><ce:surname>Dreher</ce:surname><ce:given-name>T.W.</ce:given-name></sb:author></sb:authors><sb:title><sb:maintitle>The TYMV tRNA-like structure</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Biochimie</sb:maintitle></sb:title><sb:volume-nr>75</sb:volume-nr></sb:series><sb:date>1993</sb:date></sb:issue><sb:pages><sb:first-page>569</sb:first-page><sb:last-page>582</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib19"><ce:label>[19]</ce:label><sb:reference><sb:contribution langtype="en"><sb:authors><sb:author><ce:surname>Florentz</ce:surname><ce:given-name>C.</ce:given-name></sb:author><sb:author><ce:surname>Briand</ce:surname><ce:given-name>J.P.</ce:given-name></sb:author><sb:author><ce:surname>Romby</ce:surname><ce:given-name>P.</ce:given-name></sb:author><sb:author><ce:surname>Hirth</ce:surname><ce:given-name>L.</ce:given-name></sb:author><sb:author><ce:surname>Ebel</ce:surname><ce:given-name>J.P.</ce:given-name></sb:author><sb:author><ce:surname>Giegé</ce:surname><ce:given-name>R.</ce:given-name></sb:author></sb:authors><sb:title><sb:maintitle>The tRNA-like structure of turnip yellow mosaic virus RNA: Structural organization of the last 159 nucleotides form the 3′OH terminus</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>EMBO J.</sb:maintitle></sb:title><sb:volume-nr>1</sb:volume-nr></sb:series><sb:date>1982</sb:date></sb:issue><sb:pages><sb:first-page>269</sb:first-page><sb:last-page>276</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib20"><ce:label>[20]</ce:label><sb:reference><sb:contribution langtype="en"><sb:authors><sb:author><ce:surname>Rietveld</ce:surname><ce:given-name>K.</ce:given-name></sb:author><sb:author><ce:surname>Van Poelgeest</ce:surname><ce:given-name>R.</ce:given-name></sb:author><sb:author><ce:surname>Pleij</ce:surname><ce:given-name>C.W.A.</ce:given-name></sb:author><sb:author><ce:surname>VanBoom</ce:surname><ce:given-name>J.H.</ce:given-name></sb:author><sb:author><ce:surname>Bosh</ce:surname><ce:given-name>L.</ce:given-name></sb:author></sb:authors><sb:title><sb:maintitle>The tRNA-like structure at the 3′ terminus of turnip yellow mosaic virus RNA</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:title><sb:maintitle>Differences and similarities with canonical tRNA</sb:maintitle></sb:title><sb:series><sb:title><sb:maintitle>Nucleic Acids Res.</sb:maintitle></sb:title><sb:volume-nr>10</sb:volume-nr></sb:series><sb:date>1982</sb:date></sb:issue><sb:pages><sb:first-page>1929</sb:first-page><sb:last-page>1946</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib21"><ce:label>[21]</ce:label><sb:reference><sb:contribution langtype="en"><sb:authors><sb:author><ce:surname>Rietveld</ce:surname><ce:given-name>K.</ce:given-name></sb:author><sb:author><ce:surname>Pleij</ce:surname><ce:given-name>C.W.A.</ce:given-name></sb:author><sb:author><ce:surname>Bosch</ce:surname><ce:given-name>L.</ce:given-name></sb:author></sb:authors><sb:title><sb:maintitle>Three-dimensional models of the tRNA-like 3′ termini of some plant viral RNAs</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>EMBO J.</sb:maintitle></sb:title><sb:volume-nr>2</sb:volume-nr></sb:series><sb:date>1983</sb:date></sb:issue><sb:pages><sb:first-page>1079</sb:first-page><sb:last-page>1085</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib22"><ce:label>[22]</ce:label><sb:reference><sb:contribution langtype="en"><sb:authors><sb:author><ce:surname>Dumas</ce:surname><ce:given-name>P.</ce:given-name></sb:author><sb:author><ce:surname>Moras</ce:surname><ce:given-name>D.</ce:given-name></sb:author><sb:author><ce:surname>Florentz</ce:surname><ce:given-name>C.</ce:given-name></sb:author><sb:author><ce:surname>Giegé</ce:surname><ce:given-name>R.</ce:given-name></sb:author><sb:author><ce:surname>Verlaan</ce:surname><ce:given-name>P.</ce:given-name></sb:author><sb:author><ce:surname>VanBelkum</ce:surname><ce:given-name>A.</ce:given-name></sb:author><sb:author><ce:surname>Pleij</ce:surname><ce:given-name>C.W.A.</ce:given-name></sb:author></sb:authors><sb:title><sb:maintitle>3-D graphics modelling of the tRNA-like 3′-end of turnip yellow mosaic virus RNA: structural and functional implications</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>J. Biomol. Struct. Dyn.</sb:maintitle></sb:title><sb:volume-nr>4</sb:volume-nr></sb:series><sb:date>1987</sb:date></sb:issue><sb:pages><sb:first-page>707</sb:first-page><sb:last-page>728</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib23"><ce:label>[23]</ce:label><sb:reference><sb:contribution langtype="en"><sb:authors><sb:author><ce:surname>Haenni</ce:surname><ce:given-name>A.L.</ce:given-name></sb:author><sb:author><ce:surname>Benicourt</ce:surname><ce:given-name>C.</ce:given-name></sb:author><sb:author><ce:surname>Teixeira</ce:surname><ce:given-name>S.</ce:given-name></sb:author><sb:author><ce:surname>Prochiantz</ce:surname><ce:given-name>A.</ce:given-name></sb:author><sb:author><ce:surname>Chapeville</ce:surname><ce:given-name>F.</ce:given-name></sb:author></sb:authors><sb:title><sb:maintitle>The specific role of tRNAs and tRNA-like structures in viral RNA genome replication and translation</sb:maintitle></sb:title></sb:contribution><sb:host><sb:edited-book><sb:book-series><sb:series><sb:title><sb:maintitle>FEBS Proc. Meet.</sb:maintitle></sb:title><sb:volume-nr>39</sb:volume-nr></sb:series></sb:book-series><sb:date>1975</sb:date></sb:edited-book><sb:pages><sb:first-page>121</sb:first-page><sb:last-page>131</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib24"><ce:label>[24]</ce:label><sb:reference><sb:contribution langtype="en"><sb:authors><sb:author><ce:surname>Becker</ce:surname><ce:given-name>H.D.</ce:given-name></sb:author><sb:author><ce:surname>Giegé</ce:surname><ce:given-name>R.</ce:given-name></sb:author><sb:author><ce:surname>Kern</ce:surname><ce:given-name>D.</ce:given-name></sb:author></sb:authors><sb:title><sb:maintitle>Identity of prokaryotic and eukaryotic tRNA<ce:sup loc="post">Asp</ce:sup> for aminoacylation by aspartyl-tRNA synthetase from <ce:italic>Thermus thermophilus</ce:italic></sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Biochemistry</sb:maintitle></sb:title><sb:volume-nr>35</sb:volume-nr></sb:series><sb:date>1996</sb:date></sb:issue><sb:pages><sb:first-page>7447</sb:first-page><sb:last-page>7458</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib25"><ce:label>[25]</ce:label><sb:reference><sb:contribution langtype="en"><sb:authors><sb:author><ce:surname>Hiramaru</ce:surname><ce:given-name>M.</ce:given-name></sb:author><sb:author><ce:surname>Uschida</ce:surname><ce:given-name>T.</ce:given-name></sb:author><sb:author><ce:surname>Egami</ce:surname><ce:given-name>F.</ce:given-name></sb:author></sb:authors><sb:title><sb:maintitle>Ribonuclease preparation for the base analysis of polyribonucleotides</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Anal. Biochem.</sb:maintitle></sb:title><sb:volume-nr>17</sb:volume-nr></sb:series><sb:date>1966</sb:date></sb:issue><sb:pages><sb:first-page>135</sb:first-page><sb:last-page>142</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib26"><ce:label>[26]</ce:label><sb:reference><sb:contribution langtype="en"><sb:authors><sb:author><ce:surname>Dreher</ce:surname><ce:given-name>T.</ce:given-name></sb:author><sb:author><ce:surname>Florentz</ce:surname><ce:given-name>C.</ce:given-name></sb:author><sb:author><ce:surname>Giegé</ce:surname><ce:given-name>R.</ce:given-name></sb:author></sb:authors><sb:title><sb:maintitle>Valylation of tRNA-like transcripts from cloned cDNA of turnip yellow mosaic virus RNA demonstrate that the L-shaped region at the 3′-end of the viral RNA is not sufficient for optimal aminoacylation</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Biochimie</sb:maintitle></sb:title><sb:volume-nr>70</sb:volume-nr></sb:series><sb:date>1988</sb:date></sb:issue><sb:pages><sb:first-page>1719</sb:first-page><sb:last-page>1727</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib27"><ce:label>[27]</ce:label><sb:reference><sb:contribution langtype="en"><sb:authors><sb:author><ce:surname>Grosjean</ce:surname><ce:given-name>H.</ce:given-name></sb:author><sb:author><ce:surname>Kubli</ce:surname><ce:given-name>E.</ce:given-name></sb:author></sb:authors><sb:title><sb:maintitle>Functional aspects of tRNA microinjected into <ce:italic>Xenopus laevis</ce:italic> oocytes: Results and perspectives</sb:maintitle></sb:title></sb:contribution><sb:host><sb:edited-book><sb:editors><sb:editor><ce:surname>Celis</ce:surname><ce:given-name>J.E.</ce:given-name></sb:editor><sb:editor><ce:surname>Graessman</ce:surname><ce:given-name>A.</ce:given-name></sb:editor><sb:editor><ce:surname>Loyter</ce:surname><ce:given-name>A.</ce:given-name></sb:editor></sb:editors><sb:title><sb:maintitle>Microinjection and Organelle Transplantation Techniques: Methods and Application</sb:maintitle></sb:title><sb:date>1986</sb:date><sb:publisher><sb:name>Academic Press</sb:name><sb:location>Washington, D.C.</sb:location></sb:publisher></sb:edited-book><sb:pages><sb:first-page>301</sb:first-page><sb:last-page>326</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib28"><ce:label>[28]</ce:label><sb:reference><sb:contribution langtype="en"><sb:authors><sb:author><ce:surname>Nishimura</ce:surname><ce:given-name>S.</ce:given-name></sb:author></sb:authors><sb:title><sb:maintitle>Chromatographic mobilities of modified nucleotides</sb:maintitle></sb:title></sb:contribution><sb:host><sb:edited-book><sb:editors><sb:editor><ce:surname>Schimmel</ce:surname><ce:given-name>P.</ce:given-name></sb:editor><sb:editor><ce:surname>Soll</ce:surname><ce:given-name>D.</ce:given-name></sb:editor><sb:editor><ce:surname>Abelson</ce:surname><ce:given-name>J.N.</ce:given-name></sb:editor></sb:editors><sb:title><sb:maintitle>Transfer RNA: Structure, Properties and Recognition</sb:maintitle></sb:title><sb:date>1979</sb:date><sb:publisher><sb:name>Cold Spring Harbour Laboratory</sb:name><sb:location>London</sb:location></sb:publisher></sb:edited-book><sb:pages><sb:first-page>59</sb:first-page><sb:last-page>79</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib29"><ce:label>[29]</ce:label><sb:reference><sb:contribution langtype="en"><sb:authors><sb:author><ce:surname>Keith</ce:surname><ce:given-name>G.</ce:given-name></sb:author></sb:authors><sb:title><sb:maintitle>Mobilities of modified ribonucleotides on two-dimensional cellulose thin-layer chromatography</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Biochimie</sb:maintitle></sb:title><sb:volume-nr>77</sb:volume-nr></sb:series><sb:date>1995</sb:date></sb:issue><sb:pages><sb:first-page>142</sb:first-page><sb:last-page>144</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib30"><ce:label>[30]</ce:label><sb:reference><sb:contribution langtype="en"><sb:authors><sb:author><ce:surname>Sprinzl</ce:surname><ce:given-name>M.</ce:given-name></sb:author><sb:author><ce:surname>Horn</ce:surname><ce:given-name>C.</ce:given-name></sb:author><sb:author><ce:surname>Brown</ce:surname><ce:given-name>M.</ce:given-name></sb:author><sb:author><ce:surname>Iodovitch</ce:surname><ce:given-name>A.</ce:given-name></sb:author><sb:author><ce:surname>Steinberg</ce:surname><ce:given-name>S.</ce:given-name></sb:author></sb:authors><sb:title><sb:maintitle>Compilation of tRNA sequences and sequences of tRNA genes</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Nucleic Acids Res.</sb:maintitle></sb:title><sb:volume-nr>26</sb:volume-nr></sb:series><sb:date>1998</sb:date></sb:issue><sb:pages><sb:first-page>148</sb:first-page><sb:last-page>153</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib31"><ce:label>[31]</ce:label><sb:reference><sb:contribution langtype="en"><sb:authors><sb:author><ce:surname>Grosjean</ce:surname><ce:given-name>H.</ce:given-name></sb:author><sb:author><ce:surname>Droogmans</ce:surname><ce:given-name>L.</ce:given-name></sb:author><sb:author><ce:surname>Giegé</ce:surname><ce:given-name>R.</ce:given-name></sb:author><sb:author><ce:surname>Uhlenbeck</ce:surname><ce:given-name>O.C.</ce:given-name></sb:author></sb:authors><sb:title><sb:maintitle>Guanosine modifications in runoff transcripts of synthetic transfer RNA-Phe genes microinjected into <ce:italic>Xenopus oocytes</ce:italic></sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Biochem. Biophys. Acta</sb:maintitle></sb:title><sb:volume-nr>1050</sb:volume-nr></sb:series><sb:date>1990</sb:date></sb:issue><sb:pages><sb:first-page>267</sb:first-page><sb:last-page>273</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib32"><ce:label>[32]</ce:label><sb:reference><sb:contribution langtype="en"><sb:authors><sb:author><ce:surname>Sturchler</ce:surname><ce:given-name>C.</ce:given-name></sb:author><sb:author><ce:surname>Lescure</ce:surname><ce:given-name>A.</ce:given-name></sb:author><sb:author><ce:surname>Keith</ce:surname><ce:given-name>G.</ce:given-name></sb:author><sb:author><ce:surname>Carbon</ce:surname><ce:given-name>P.</ce:given-name></sb:author><sb:author><ce:surname>Krol</ce:surname><ce:given-name>A.</ce:given-name></sb:author></sb:authors><sb:title><sb:maintitle>Base modification pattern at the wobble position of <ce:italic>Xenopus</ce:italic> selenocysteine tRNA<ce:sup loc="post">Sec</ce:sup></sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Nucleic Acids Res.</sb:maintitle></sb:title><sb:volume-nr>22</sb:volume-nr></sb:series><sb:date>1994</sb:date></sb:issue><sb:pages><sb:first-page>1354</sb:first-page><sb:last-page>1358</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib33"><ce:label>[33]</ce:label><sb:reference><sb:contribution langtype="en"><sb:authors><sb:author><ce:surname>Nishikura</ce:surname><ce:given-name>K.</ce:given-name></sb:author><sb:author><ce:surname>DeRobertis</ce:surname><ce:given-name>E.M.</ce:given-name></sb:author></sb:authors><sb:title><sb:maintitle>RNA processing in microinjected <ce:italic>Xenopus oocytes</ce:italic>: sequential addition of base modifications in a spliced tRNA</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>J. Mol. Biol.</sb:maintitle></sb:title><sb:volume-nr>145</sb:volume-nr></sb:series><sb:date>1981</sb:date></sb:issue><sb:pages><sb:first-page>405</sb:first-page><sb:last-page>420</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib34"><ce:label>[34]</ce:label><sb:reference><sb:contribution langtype="en"><sb:authors><sb:author><ce:surname>Rudinger</ce:surname><ce:given-name>J.</ce:given-name></sb:author><sb:author><ce:surname>Flroetnz</ce:surname><ce:given-name>C.</ce:given-name></sb:author><sb:author><ce:surname>Giegé</ce:surname><ce:given-name>R.</ce:given-name></sb:author></sb:authors><sb:title><sb:maintitle>Histidylation by yeast MsRS of tRNA or IRNA-like structure relies on residues -1 and 73, but is dependent on the RNA context</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Nucleic Acids Res.</sb:maintitle></sb:title><sb:volume-nr>22</sb:volume-nr></sb:series><sb:date>1994</sb:date></sb:issue><sb:pages><sb:first-page>5031</sb:first-page><sb:last-page>5037</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib35"><ce:label>[35]</ce:label><sb:reference><sb:contribution langtype="en"><sb:authors><sb:author><ce:surname>Nishikura</ce:surname><ce:given-name>K.</ce:given-name></sb:author><sb:author><ce:surname>Kurjan</ce:surname><ce:given-name>J.</ce:given-name></sb:author><sb:author><ce:surname>Hall</ce:surname><ce:given-name>B.D.</ce:given-name></sb:author><sb:author><ce:surname>DeRobertis</ce:surname><ce:given-name>E.M.</ce:given-name></sb:author></sb:authors><sb:title><sb:maintitle>Genetic analysis of the processing of a spliced tRNA</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>EMBO J.</sb:maintitle></sb:title><sb:volume-nr>1</sb:volume-nr></sb:series><sb:date>1982</sb:date></sb:issue><sb:pages><sb:first-page>263</sb:first-page><sb:last-page>269</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib36"><ce:label>[36]</ce:label><sb:reference><sb:contribution langtype="en"><sb:authors><sb:author><ce:surname>Sakamoto</ce:surname><ce:given-name>K.</ce:given-name></sb:author><sb:author><ce:surname>Okada</ce:surname><ce:given-name>N.</ce:given-name></sb:author></sb:authors><sb:title><sb:maintitle>5-Methylcytidylic modification of in vitro transcript from the rat identifier sequence: evidence that the transcript forms a tRNA-like structure</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Nucleic Acids Res.</sb:maintitle></sb:title><sb:volume-nr>13</sb:volume-nr></sb:series><sb:date>1985</sb:date></sb:issue><sb:pages><sb:first-page>7195</sb:first-page><sb:last-page>7206</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib37"><ce:label>[37]</ce:label><sb:reference><sb:contribution langtype="en"><sb:authors><sb:author><ce:surname>Keith</ce:surname><ce:given-name>J.M.</ce:given-name></sb:author><sb:author><ce:surname>Winters</ce:surname><ce:given-name>E.M.</ce:given-name></sb:author><sb:author><ce:surname>Moss</ce:surname><ce:given-name>B.</ce:given-name></sb:author></sb:authors><sb:title><sb:maintitle>Purification and characterization of a HeLa cell transfer RNA (cytosine-5-)-methyltransferase</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>J. Biol. Chem.</sb:maintitle></sb:title><sb:volume-nr>255</sb:volume-nr></sb:series><sb:date>1980</sb:date></sb:issue><sb:pages><sb:first-page>4636</sb:first-page><sb:last-page>4644</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib38"><ce:label>[38]</ce:label><sb:reference><sb:contribution langtype="en"><sb:authors><sb:author><ce:surname>Becker</ce:surname><ce:given-name>H.D.</ce:given-name></sb:author><sb:author><ce:surname>Motorin</ce:surname><ce:given-name>Y.</ce:given-name></sb:author><sb:author><ce:surname>Florentz</ce:surname><ce:given-name>C.</ce:given-name></sb:author><sb:author><ce:surname>Giegé</ce:surname><ce:given-name>R.</ce:given-name></sb:author><sb:author><ce:surname>Grosjean</ce:surname><ce:given-name>H.</ce:given-name></sb:author></sb:authors><sb:title><sb:maintitle>Pseudouridine and ribothymidine formation in the tRNA-like domain of turnip yellow mosaic virus RNA</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Nucleic Acids Res.</sb:maintitle></sb:title><sb:volume-nr>26</sb:volume-nr></sb:series><sb:date>1998</sb:date></sb:issue><sb:pages><sb:first-page>3991</sb:first-page><sb:last-page>3997</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib39"><ce:label>[39]</ce:label><sb:reference><sb:contribution langtype="en"><sb:authors><sb:author><ce:surname>Gu</ce:surname><ce:given-name>X.</ce:given-name></sb:author><sb:author><ce:surname>Ivanetich</ce:surname><ce:given-name>K.M.</ce:given-name></sb:author><sb:author><ce:surname>Santi</ce:surname><ce:given-name>D.V.</ce:given-name></sb:author></sb:authors><sb:title><sb:maintitle>Recognition of the T-arm of tRNA by tRNA (m<ce:sup loc="post">5</ce:sup>U54)-methyltransferase is not sequence specific</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Biochemistry</sb:maintitle></sb:title><sb:volume-nr>35</sb:volume-nr></sb:series><sb:date>1996</sb:date></sb:issue><sb:pages><sb:first-page>11652</sb:first-page><sb:last-page>11659</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib40"><ce:label>[40]</ce:label><sb:reference><sb:contribution langtype="en"><sb:authors><sb:author><ce:surname>Mans</ce:surname><ce:given-name>R.M.W.</ce:given-name></sb:author><sb:author><ce:surname>Verlaan</ce:surname><ce:given-name>P.</ce:given-name></sb:author><sb:author><ce:surname>Pleij</ce:surname><ce:given-name>C.W.A.</ce:given-name></sb:author><sb:author><ce:surname>Bosch</ce:surname><ce:given-name>L.</ce:given-name></sb:author></sb:authors><sb:title><sb:maintitle>Aminoacylation of 3′-terminal tRNA-like fragments of Turnip Yellow Mosaic Virus RNA: the influence of 5′ non-viral sequences</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Biochem. Biophys. Arch.</sb:maintitle></sb:title><sb:volume-nr>1050</sb:volume-nr></sb:series><sb:date>1990</sb:date></sb:issue><sb:pages><sb:first-page>186</sb:first-page><sb:last-page>192</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib41"><ce:label>[41]</ce:label><sb:reference><sb:contribution langtype="en"><sb:authors><sb:author><ce:surname>Bokar</ce:surname><ce:given-name>J.A.</ce:given-name></sb:author><sb:author><ce:surname>Rottman</ce:surname><ce:given-name>E.M.</ce:given-name></sb:author></sb:authors><sb:title><sb:maintitle>Biosynthesis and functions of modified nucleosides in eukaryotic mRNA</sb:maintitle></sb:title></sb:contribution><sb:host><sb:edited-book><sb:editors><sb:editor><ce:surname>Grosjean</ce:surname><ce:given-name>H.</ce:given-name></sb:editor><sb:editor><ce:surname>Benne</ce:surname><ce:given-name>R.</ce:given-name></sb:editor></sb:editors><sb:title><sb:maintitle>Modification and Editing of RNA</sb:maintitle></sb:title><sb:date>1998</sb:date><sb:publisher><sb:name>ASM Press</sb:name><sb:location>Cold Spring Harbour, NY</sb:location></sb:publisher></sb:edited-book><sb:pages><sb:first-page>183</sb:first-page><sb:last-page>200</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib42"><ce:label>[42]</ce:label><sb:reference><sb:contribution langtype="en"><sb:authors><sb:author><ce:surname>Joshi</ce:surname><ce:given-name>S.</ce:given-name></sb:author><sb:author><ce:surname>Haenni</ce:surname><ce:given-name>A.L.</ce:given-name></sb:author><sb:author><ce:surname>Hubert</ce:surname><ce:given-name>E.</ce:given-name></sb:author><sb:author><ce:surname>Huez</ce:surname><ce:given-name>G.</ce:given-name></sb:author><sb:author><ce:surname>Marbaix</ce:surname><ce:given-name>G.</ce:given-name></sb:author></sb:authors><sb:title><sb:maintitle>In vivo aminoacylation and ‘processing’ of turnip yellow mosaic virus RNA in <ce:italic>Xenopus laevis</ce:italic> oocytes</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Nature</sb:maintitle></sb:title><sb:volume-nr>275</sb:volume-nr></sb:series><sb:date>1978</sb:date></sb:issue><sb:pages><sb:first-page>339</sb:first-page><sb:last-page>341</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib43"><ce:label>[43]</ce:label><sb:reference><sb:contribution langtype="en"><sb:authors><sb:author><ce:surname>Marcu</ce:surname><ce:given-name>K.</ce:given-name></sb:author><sb:author><ce:surname>Dudock</ce:surname><ce:given-name>B.</ce:given-name></sb:author></sb:authors><sb:title><sb:maintitle>Methylation of TMV RNA</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Biochim. Biophys. Res. Commun.</sb:maintitle></sb:title><sb:volume-nr>62</sb:volume-nr></sb:series><sb:date>1975</sb:date></sb:issue><sb:pages><sb:first-page>798</sb:first-page><sb:last-page>807</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib44"><ce:label>[44]</ce:label><sb:reference><sb:contribution langtype="en"><sb:authors><sb:author><ce:surname>Lesiewicz</ce:surname><ce:given-name>J.</ce:given-name></sb:author><sb:author><ce:surname>Dudock</ce:surname><ce:given-name>B.</ce:given-name></sb:author></sb:authors><sb:title><sb:maintitle>In vitro methylation of tobacco mosaic virus RNA with ribothymidine-forming tRNA methyltransferase</sb:maintitle></sb:title></sb:contribution><sb:host><sb:issue><sb:title><sb:maintitle>Characterization and specificity of the reaction</sb:maintitle></sb:title><sb:series><sb:title><sb:maintitle>Biochim. Biophys. Acta</sb:maintitle></sb:title><sb:volume-nr>520</sb:volume-nr></sb:series><sb:date>1978</sb:date></sb:issue><sb:pages><sb:first-page>411</sb:first-page><sb:last-page>418</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib45"><ce:label>[45]</ce:label><sb:reference><sb:host><sb:edited-book><sb:editors><sb:editor><ce:surname>Grosjean</ce:surname><ce:given-name>H.</ce:given-name></sb:editor><sb:editor><ce:surname>Benne</ce:surname><ce:given-name>R.</ce:given-name></sb:editor></sb:editors><sb:title><sb:maintitle>Modification and editing of RNA</sb:maintitle></sb:title><sb:date>1998</sb:date><sb:publisher><sb:name>ASM Press</sb:name><sb:location>Washington, D.C.</sb:location></sb:publisher></sb:edited-book></sb:host></sb:reference></ce:bib-reference></ce:bibliography-sec></ce:bibliography></tail></article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>A pseudoknotted tRNA variant is a substrate for tRNA (cytosine-5)-methyltransferase from Xenopus laevis</title></titleInfo><titleInfo type="alternative" lang="en" contentType="CDATA"><title>A pseudoknotted tRNA variant is a substrate for tRNA (cytosine-5)-methyltransferase from</title></titleInfo><name type="personal"><namePart type="given">Hervé</namePart><namePart type="family">Brulé</namePart><affiliation>UPR 9002 du CNRS, Institut de Biologie Moléculaire et Cellulaire, 15, rue René-Descartes, 67084 Strasbourg cedex, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Henri</namePart><namePart type="family">Grosjean</namePart><affiliation>Laboratoire d'Enzymologie et Biochimie Structurales du CNRS, 1, avenue de la Terrasse, 91198 Gif-Sur-Yvette, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Richard</namePart><namePart type="family">Giegé</namePart><affiliation>UPR 9002 du CNRS, Institut de Biologie Moléculaire et Cellulaire, 15, rue René-Descartes, 67084 Strasbourg cedex, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Catherine</namePart><namePart type="family">Florentz</namePart><affiliation>UPR 9002 du CNRS, Institut de Biologie Moléculaire et Cellulaire, 15, rue René-Descartes, 67084 Strasbourg cedex, France</affiliation><affiliation>Correspondence and reprints</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1998</dateIssued><copyrightDate encoding="w3cdtf">1998</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: tRNA post-transcriptional modification enzymes of Xenopus laevis were proposed previously to belong to two major groups according to their sensitivity to structural perturbations in their substrates. To further investigate the structural variations tolerated by these enzymes, the tRNA-like domain of turnip yellow mosaic virus RNA (88 nucleotides in length) has been microinjected into the oocytes of Xenopus laevis. This RNA possesses 12 potential target nucleotides for modification within a structure including a pseudoknotted folding, an extended anticodon stem, and unusual D-loop/T-loop interactions. Results indicate that only cytosine-42, a position equivalent to C-49 in canonical tRNAs, was quantitatively modified into m5C in the microinjected RNA. Modification was detected to high levels, indicating that at least one enzyme tolerates non-canonical structural features.</abstract><subject lang="en"><topic>tRNA</topic><topic>post-transcriptional modification</topic><topic>turnip yellow mosaic virus</topic><topic>methylase</topic><topic>tertiary structure</topic><topic>Xenopus laevis</topic></subject><subject lang="en"><genre>Abbreviations</genre><topic>TYMV : turnip yellow mosaic virus</topic><topic>TLC : thin layer chromatography</topic><topic>cps : counts per second</topic></subject><relatedItem type="host"><titleInfo><title>Biochimie</title></titleInfo><titleInfo type="abbreviated"><title>BIOCHI</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1998</dateIssued></originInfo><identifier type="ISSN">0300-9084</identifier><identifier type="PII">S0300-9084(00)X0194-0</identifier><part><date>1998</date><detail type="volume"><number>80</number><caption>vol.</caption></detail><detail type="issue"><number>12</number><caption>no.</caption></detail><extent unit="issue-pages"><start>963</start><end>1080</end></extent><extent unit="pages"><start>977</start><end>985</end></extent></part></relatedItem><identifier type="istex">02400B0AE40FC063AB70C507AC2E17A605294A4D</identifier><identifier type="ark">ark:/67375/6H6-8WH36MQS-D</identifier><identifier type="DOI">10.1016/S0300-9084(99)80003-0</identifier><identifier type="PII">S0300-9084(99)80003-0</identifier><identifier type="ArticleID">99800030</identifier><accessCondition type="use and reproduction" contentType="copyright">©1998 Société française de biochimie et biologie moléculaire/ Elsevier, Paris</accessCondition><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M">elsevier</recordContentSource><recordOrigin>Société française de biochimie et biologie moléculaire/ Elsevier, Paris, ©1998</recordOrigin></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-8WH36MQS-D/record.json</uri></json:item></metadata></istex></record>Pour manipuler ce document sous Unix (Dilib)
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