Conformation in solution of yeast tRNAAsp transcripts deprived of modified nucleotides
Identifieur interne : 001E38 ( Istex/Corpus ); précédent : 001E37; suivant : 001E39Conformation in solution of yeast tRNAAsp transcripts deprived of modified nucleotides
Auteurs : V. Perret ; A. Garcia ; J. Puglisi ; H. Grosjean ; J. P. Ebel ; C. Florentz ; R. GiegéSource :
- Biochimie [ 0300-9084 ] ; 1990.
English descriptors
- Teeft :
- Active conformations, Alkaline hydrolysis ladders, Aminoacylation, Base pair, Biol, Biol chem, Bold characters, Chemical probes, Cleavage, Cleavage experiments, Comparative chemical mapping, Comparative experiments, Conformation, Conformational, Conformational change, Conformational changes, Denaturing conditions, Diethyl pyrocarbonate, Dimethyl, Dimethyl sulphate, Ebel, Escherichia coli, Functional implications, Gieg6, Incorrect aminoacylations, Modification, Molecule, Moras, Native conditions, Native trna, Native trnaasp, Nucleic acids, Nucleotide, Oligonucleotides, Polymerase, Polynucleotide kinase, Proc natl acad, Promoter extension, Recherche scientifique, Sodium cacodylate, Structural mapping, Structural plasticity, Sulphate, Synthetase, Synthetic gene, Synthetic genes, Tertiary structure, Thermal stability, Transcript, Transcription, Transcriptional medium, Trna, Trna genes, Trna sequence, Trnaasp, Trnaasp molecules, Unmodified, Unmodified molecules, Unmodified transcript, Unmodified transcripts, Unmodified trnaasp, Unmodified trnaasp transcripts, Unmodified trnas, Yeast, Yeast phenylalanine transfer, Yeast trna, Yeast trnaasp, Yeast trnaasp transcripts.
Abstract
Abstract: A synthetic gene of yeast aspartic acid tRNA with a promoter for phage T7 RNA polymerase was cloned in Escherichia coli. The in vitro transcribed tRNAAsp molecules are deprived of modified nucleotides and retain their aspartylation capacity. The solution conformation of these molecules was mapped with chemical structural probes and compared to that of fully modified molecules. Significant differences in reactivities were observed in Pb2+ cleavage of the RNAs and in modification of the bases with dimethyl sulphate. The most striking result concerns C56, which becomes reactive in unmodified tRNAAsp, indicating the disruption of the C56-G19 base pair involved in the D- and T-loop interaction. The chemical data indicate that unmodified tRNAAsp transcripts possess a relaxed conformation compared to that of the native tRNA. This conclusion is confirmed by thermal melting experiments. Thus it can be proposed that post-transcriptional modifications of nucleotides in tRNA stabilize the biologically active conformations in these molecules.
Url:
DOI: 10.1016/0300-9084(90)90158-D
Links to Exploration step
ISTEX:87A0DD688E17D2C2BCD3003336CD37F4F786D175Le document en format XML
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Ebel</name><affiliation><mods:affiliation>Laboratoire de Biochimie, Institut de Biologie Moléculaire et Cellulaire, Centre National de la Recherche Scientifique 15, rue René Descartes, F-67084 Strasbourg Cedex, France</mods:affiliation></affiliation></author><author><name sortKey="Florentz, C" sort="Florentz, C" uniqKey="Florentz C" first="C." last="Florentz">C. Florentz</name><affiliation><mods:affiliation>Laboratoire de Biochimie, Institut de Biologie Moléculaire et Cellulaire, Centre National de la Recherche Scientifique 15, rue René Descartes, F-67084 Strasbourg Cedex, France</mods:affiliation></affiliation></author><author><name sortKey="Giege, R" sort="Giege, R" uniqKey="Giege R" first="R." last="Giegé">R. 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The in vitro transcribed tRNAAsp molecules are deprived of modified nucleotides and retain their aspartylation capacity. The solution conformation of these molecules was mapped with chemical structural probes and compared to that of fully modified molecules. Significant differences in reactivities were observed in Pb2+ cleavage of the RNAs and in modification of the bases with dimethyl sulphate. The most striking result concerns C56, which becomes reactive in unmodified tRNAAsp, indicating the disruption of the C56-G19 base pair involved in the D- and T-loop interaction. The chemical data indicate that unmodified tRNAAsp transcripts possess a relaxed conformation compared to that of the native tRNA. This conclusion is confirmed by thermal melting experiments. Thus it can be proposed that post-transcriptional modifications of nucleotides in tRNA stabilize the biologically active conformations in these molecules.</div></front></TEI><istex><corpusName>elsevier</corpusName><keywords><teeft><json:string>trna</json:string><json:string>trnaasp</json:string><json:string>unmodified</json:string><json:string>sulphate</json:string><json:string>dimethyl</json:string><json:string>synthetase</json:string><json:string>gieg6</json:string><json:string>polymerase</json:string><json:string>ebel</json:string><json:string>dimethyl sulphate</json:string><json:string>yeast trnaasp</json:string><json:string>aminoacylation</json:string><json:string>moras</json:string><json:string>oligonucleotides</json:string><json:string>biol</json:string><json:string>transcript</json:string><json:string>yeast trna</json:string><json:string>nucleic acids</json:string><json:string>proc natl acad</json:string><json:string>unmodified trnaasp</json:string><json:string>unmodified trnaasp transcripts</json:string><json:string>yeast</json:string><json:string>native conditions</json:string><json:string>conformational changes</json:string><json:string>conformational change</json:string><json:string>conformation</json:string><json:string>cleavage</json:string><json:string>conformational</json:string><json:string>modification</json:string><json:string>nucleotide</json:string><json:string>native trna</json:string><json:string>diethyl pyrocarbonate</json:string><json:string>sodium cacodylate</json:string><json:string>denaturing conditions</json:string><json:string>unmodified molecules</json:string><json:string>cleavage experiments</json:string><json:string>native trnaasp</json:string><json:string>unmodified transcript</json:string><json:string>synthetic gene</json:string><json:string>escherichia coli</json:string><json:string>unmodified trnas</json:string><json:string>molecule</json:string><json:string>trnaasp molecules</json:string><json:string>polynucleotide kinase</json:string><json:string>alkaline hydrolysis ladders</json:string><json:string>promoter extension</json:string><json:string>trna sequence</json:string><json:string>yeast phenylalanine transfer</json:string><json:string>comparative chemical mapping</json:string><json:string>base pair</json:string><json:string>structural mapping</json:string><json:string>trna genes</json:string><json:string>thermal stability</json:string><json:string>bold characters</json:string><json:string>biol chem</json:string><json:string>chemical probes</json:string><json:string>synthetic genes</json:string><json:string>tertiary structure</json:string><json:string>functional implications</json:string><json:string>structural plasticity</json:string><json:string>comparative experiments</json:string><json:string>incorrect aminoacylations</json:string><json:string>unmodified transcripts</json:string><json:string>recherche scientifique</json:string><json:string>active conformations</json:string><json:string>yeast trnaasp transcripts</json:string><json:string>transcriptional medium</json:string><json:string>transcription</json:string></teeft></keywords><author><json:item><name>V. Perret</name><affiliations><json:string>Laboratoire de Biochimie, Institut de Biologie Moléculaire et Cellulaire, Centre National de la Recherche Scientifique 15, rue René Descartes, F-67084 Strasbourg Cedex, France</json:string></affiliations></json:item><json:item><name>A. Garcia</name><affiliations><json:string>Laboratoire de Biochimie, Institut de Biologie Moléculaire et Cellulaire, Centre National de la Recherche Scientifique 15, rue René Descartes, F-67084 Strasbourg Cedex, France</json:string></affiliations></json:item><json:item><name>J. Puglisi</name><affiliations><json:string>Laboratoire de Biochimie, Institut de Biologie Moléculaire et Cellulaire, Centre National de la Recherche Scientifique 15, rue René Descartes, F-67084 Strasbourg Cedex, France</json:string></affiliations></json:item><json:item><name>H. Grosjean</name><affiliations><json:string>Laboratoire de Biochimie, Institut de Biologie Moléculaire et Cellulaire, Centre National de la Recherche Scientifique 15, rue René Descartes, F-67084 Strasbourg Cedex, France</json:string></affiliations></json:item><json:item><name>J.P. Ebel</name><affiliations><json:string>Laboratoire de Biochimie, Institut de Biologie Moléculaire et Cellulaire, Centre National de la Recherche Scientifique 15, rue René Descartes, F-67084 Strasbourg Cedex, France</json:string></affiliations></json:item><json:item><name>C. Florentz</name><affiliations><json:string>Laboratoire de Biochimie, Institut de Biologie Moléculaire et Cellulaire, Centre National de la Recherche Scientifique 15, rue René Descartes, F-67084 Strasbourg Cedex, France</json:string></affiliations></json:item><json:item><name>R. Giegé</name><affiliations><json:string>Laboratoire de Biochimie, Institut de Biologie Moléculaire et Cellulaire, Centre National de la Recherche Scientifique 15, rue René Descartes, F-67084 Strasbourg Cedex, France</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>tRNAAsp transcripts</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>chemical RNA probes</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>thermal RNA melting</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>RNA conformation</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>modified nucleotides</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>NTP : nucleoside triphosphate (N = A, G, U, C)</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>DTE : dithioerythritol</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>EDTA : ethylendiaminetetraacetic acid</value></json:item></subject><arkIstex>ark:/67375/6H6-R6M7RKB8-V</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>Abstract: A synthetic gene of yeast aspartic acid tRNA with a promoter for phage T7 RNA polymerase was cloned in Escherichia coli. The in vitro transcribed tRNAAsp molecules are deprived of modified nucleotides and retain their aspartylation capacity. The solution conformation of these molecules was mapped with chemical structural probes and compared to that of fully modified molecules. Significant differences in reactivities were observed in Pb2+ cleavage of the RNAs and in modification of the bases with dimethyl sulphate. The most striking result concerns C56, which becomes reactive in unmodified tRNAAsp, indicating the disruption of the C56-G19 base pair involved in the D- and T-loop interaction. The chemical data indicate that unmodified tRNAAsp transcripts possess a relaxed conformation compared to that of the native tRNA. This conclusion is confirmed by thermal melting experiments. Thus it can be proposed that post-transcriptional modifications of nucleotides in tRNA stabilize the biologically active conformations in these molecules.</abstract><qualityIndicators><score>8.569</score><pdfWordCount>4733</pdfWordCount><pdfCharCount>29636</pdfCharCount><pdfVersion>1.2</pdfVersion><pdfPageCount>9</pdfPageCount><pdfPageSize>591 x 764 pts</pdfPageSize><refBibsNative>true</refBibsNative><abstractWordCount>153</abstractWordCount><abstractCharCount>1055</abstractCharCount><keywordCount>8</keywordCount></qualityIndicators><title>Conformation in solution of yeast tRNAAsp transcripts deprived of modified nucleotides</title><pmid><json:string>2078590</json:string></pmid><pii><json:string>0300-9084(90)90158-D</json:string></pii><genre><json:string>research-article</json:string></genre><serie><title>Proc Natl Acad Sci 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type="first">V.</forename><surname>Perret</surname></persName><affiliation>Laboratoire de Biochimie, Institut de Biologie Moléculaire et Cellulaire, Centre National de la Recherche Scientifique 15, rue René Descartes, F-67084 Strasbourg Cedex, France</affiliation></author><author xml:id="author-0001"><persName><forename type="first">A.</forename><surname>Garcia</surname></persName><affiliation>Laboratoire de Biochimie, Institut de Biologie Moléculaire et Cellulaire, Centre National de la Recherche Scientifique 15, rue René Descartes, F-67084 Strasbourg Cedex, France</affiliation></author><author xml:id="author-0002"><persName><forename type="first">J.</forename><surname>Puglisi</surname></persName><affiliation>Laboratoire de Biochimie, Institut de Biologie Moléculaire et Cellulaire, Centre National de la Recherche Scientifique 15, rue René Descartes, F-67084 Strasbourg Cedex, France</affiliation></author><author xml:id="author-0003"><persName><forename type="first">H.</forename><surname>Grosjean</surname></persName><affiliation>Laboratoire de Biochimie, Institut de Biologie Moléculaire et Cellulaire, Centre National de la Recherche Scientifique 15, rue René Descartes, F-67084 Strasbourg Cedex, France</affiliation></author><author xml:id="author-0004"><persName><forename type="first">J.P.</forename><surname>Ebel</surname></persName><affiliation>Laboratoire de Biochimie, Institut de Biologie Moléculaire et Cellulaire, Centre National de la Recherche Scientifique 15, rue René Descartes, F-67084 Strasbourg Cedex, France</affiliation></author><author xml:id="author-0005"><persName><forename type="first">C.</forename><surname>Florentz</surname></persName><affiliation>Laboratoire de Biochimie, Institut de Biologie Moléculaire et Cellulaire, Centre National de la Recherche Scientifique 15, rue René Descartes, F-67084 Strasbourg Cedex, France</affiliation></author><author xml:id="author-0006"><persName><forename type="first">R.</forename><surname>Giegé</surname></persName><note type="correspondence"><p>Correspondence and reprints</p></note><affiliation>Laboratoire de Biochimie, Institut de Biologie Moléculaire et Cellulaire, Centre National de la Recherche Scientifique 15, rue René Descartes, F-67084 Strasbourg Cedex, France</affiliation></author><idno type="istex">87A0DD688E17D2C2BCD3003336CD37F4F786D175</idno><idno type="ark">ark:/67375/6H6-R6M7RKB8-V</idno><idno type="DOI">10.1016/0300-9084(90)90158-D</idno><idno type="PII">0300-9084(90)90158-D</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)X0116-2</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1990"></date><biblScope unit="volume">72</biblScope><biblScope unit="issue">10</biblScope><biblScope unit="page" from="735">735</biblScope><biblScope unit="page" to="743">743</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1990</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Abstract: A synthetic gene of yeast aspartic acid tRNA with a promoter for phage T7 RNA polymerase was cloned in Escherichia coli. The in vitro transcribed tRNAAsp molecules are deprived of modified nucleotides and retain their aspartylation capacity. The solution conformation of these molecules was mapped with chemical structural probes and compared to that of fully modified molecules. Significant differences in reactivities were observed in Pb2+ cleavage of the RNAs and in modification of the bases with dimethyl sulphate. The most striking result concerns C56, which becomes reactive in unmodified tRNAAsp, indicating the disruption of the C56-G19 base pair involved in the D- and T-loop interaction. The chemical data indicate that unmodified tRNAAsp transcripts possess a relaxed conformation compared to that of the native tRNA. This conclusion is confirmed by thermal melting experiments. Thus it can be proposed that post-transcriptional modifications of nucleotides in tRNA stabilize the biologically active conformations in these molecules.</p></abstract><textClass><keywords scheme="keyword"><list><head>Keywords</head><item><term>tRNAAsp transcripts</term></item><item><term>chemical RNA probes</term></item><item><term>thermal RNA melting</term></item><item><term>RNA conformation</term></item><item><term>modified nucleotides</term></item></list></keywords></textClass><textClass><keywords scheme="keyword"><list><head>Abbreviations</head><item><term>NTP</term><term>nucleoside triphosphate (N = A, G, U, C)</term></item><item><term>DTE</term><term>dithioerythritol</term></item><item><term>EDTA</term><term>ethylendiaminetetraacetic acid</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1990">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-R6M7RKB8-V/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier, elements deleted: tail"><istex:xmlDeclaration>version="1.0" encoding="utf-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//ES//DTD journal article DTD version 4.5.2//EN//XML" URI="art452.dtd" name="istex:docType"></istex:docType><istex:document><converted-article version="4.5.2" docsubtype="fla"><item-info><jid>BIOCHI</jid><aid>9090158D</aid><ce:pii>0300-9084(90)90158-D</ce:pii><ce:doi>10.1016/0300-9084(90)90158-D</ce:doi><ce:copyright type="unknown" year="1990"></ce:copyright></item-info><head><ce:title>Conformation in solution of yeast tRNA<ce:sup>Asp</ce:sup> transcripts deprived of modified nucleotides</ce:title><ce:author-group><ce:author><ce:given-name>V.</ce:given-name><ce:surname>Perret</ce:surname></ce:author><ce:author><ce:given-name>A.</ce:given-name><ce:surname>Garcia</ce:surname></ce:author><ce:author><ce:given-name>J.</ce:given-name><ce:surname>Puglisi</ce:surname></ce:author><ce:author><ce:given-name>H.</ce:given-name><ce:surname>Grosjean</ce:surname></ce:author><ce:author><ce:given-name>J.P.</ce:given-name><ce:surname>Ebel</ce:surname></ce:author><ce:author><ce:given-name>C.</ce:given-name><ce:surname>Florentz</ce:surname></ce:author><ce:author><ce:given-name>R.</ce:given-name><ce:surname>Giegé</ce:surname><ce:cross-ref refid="COR1"><ce:sup>∗</ce:sup></ce:cross-ref></ce:author><ce:affiliation><ce:textfn>Laboratoire de Biochimie, Institut de Biologie Moléculaire et Cellulaire, Centre National de la Recherche Scientifique 15, rue René Descartes, F-67084 Strasbourg Cedex, 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="29" month="6" year="1990"></ce:date-received><ce:date-accepted day="20" month="9" year="1990"></ce:date-accepted><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>A synthetic gene of yeast aspartic acid tRNA with a promoter for phage T7 RNA polymerase was cloned in <ce:italic>Escherichia coli</ce:italic>. The <ce:italic>in vitro</ce:italic> transcribed tRNA<ce:sup>Asp</ce:sup> molecules are deprived of modified nucleotides and retain their aspartylation capacity. The solution conformation of these molecules was mapped with chemical structural probes and compared to that of fully modified molecules. Significant differences in reactivities were observed in Pb<ce:sup>2+</ce:sup> cleavage of the RNAs and in modification of the bases with dimethyl sulphate. The most striking result concerns C56, which becomes reactive in unmodified tRNA<ce:sup>Asp</ce:sup>, indicating the disruption of the C56-G19 base pair involved in the D- and T-loop interaction. The chemical data indicate that unmodified tRNA<ce:sup>Asp</ce:sup> transcripts possess a relaxed conformation compared to that of the native tRNA. This conclusion is confirmed by thermal melting experiments. Thus it can be proposed that post-transcriptional modifications of nucleotides in tRNA stabilize the biologically active conformations in these molecules.</ce:simple-para></ce:abstract-sec></ce:abstract><ce:keywords><ce:section-title>Keywords</ce:section-title><ce:keyword><ce:text>tRNA<ce:sup>Asp</ce:sup> transcripts</ce:text></ce:keyword><ce:keyword><ce:text>chemical RNA probes</ce:text></ce:keyword><ce:keyword><ce:text>thermal RNA melting</ce:text></ce:keyword><ce:keyword><ce:text>RNA conformation</ce:text></ce:keyword><ce:keyword><ce:text>modified nucleotides</ce:text></ce:keyword></ce:keywords><ce:keywords class="abr"><ce:section-title>Abbreviations</ce:section-title><ce:keyword><ce:text>NTP</ce:text><ce:keyword><ce:text>nucleoside triphosphate (N = A, G, U, C)</ce:text></ce:keyword></ce:keyword><ce:keyword><ce:text>DTE</ce:text><ce:keyword><ce:text>dithioerythritol</ce:text></ce:keyword></ce:keyword><ce:keyword><ce:text>EDTA</ce:text><ce:keyword><ce:text>ethylendiaminetetraacetic acid</ce:text></ce:keyword></ce:keyword></ce:keywords></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Conformation in solution of yeast tRNAAsp transcripts deprived of modified nucleotides</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Conformation in solution of yeast tRNA</title></titleInfo><name type="personal"><namePart type="given">V.</namePart><namePart type="family">Perret</namePart><affiliation>Laboratoire de Biochimie, Institut de Biologie Moléculaire et Cellulaire, Centre National de la Recherche Scientifique 15, rue René Descartes, F-67084 Strasbourg Cedex, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">A.</namePart><namePart type="family">Garcia</namePart><affiliation>Laboratoire de Biochimie, Institut de Biologie Moléculaire et Cellulaire, Centre National de la Recherche Scientifique 15, rue René Descartes, F-67084 Strasbourg Cedex, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">J.</namePart><namePart type="family">Puglisi</namePart><affiliation>Laboratoire de Biochimie, Institut de Biologie Moléculaire et Cellulaire, Centre National de la Recherche Scientifique 15, rue René Descartes, F-67084 Strasbourg Cedex, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">H.</namePart><namePart type="family">Grosjean</namePart><affiliation>Laboratoire de Biochimie, Institut de Biologie Moléculaire et Cellulaire, Centre National de la Recherche Scientifique 15, rue René Descartes, F-67084 Strasbourg Cedex, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">J.P.</namePart><namePart type="family">Ebel</namePart><affiliation>Laboratoire de Biochimie, Institut de Biologie Moléculaire et Cellulaire, Centre National de la Recherche Scientifique 15, rue René Descartes, F-67084 Strasbourg Cedex, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">C.</namePart><namePart type="family">Florentz</namePart><affiliation>Laboratoire de Biochimie, Institut de Biologie Moléculaire et Cellulaire, Centre National de la Recherche Scientifique 15, rue René Descartes, F-67084 Strasbourg Cedex, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">R.</namePart><namePart type="family">Giegé</namePart><affiliation>Laboratoire de Biochimie, Institut de Biologie Moléculaire et Cellulaire, Centre National de la Recherche Scientifique 15, rue René Descartes, F-67084 Strasbourg Cedex, France</affiliation><description>Correspondence and reprints</description><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">1990</dateIssued><copyrightDate encoding="w3cdtf">1990</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: A synthetic gene of yeast aspartic acid tRNA with a promoter for phage T7 RNA polymerase was cloned in Escherichia coli. The in vitro transcribed tRNAAsp molecules are deprived of modified nucleotides and retain their aspartylation capacity. The solution conformation of these molecules was mapped with chemical structural probes and compared to that of fully modified molecules. Significant differences in reactivities were observed in Pb2+ cleavage of the RNAs and in modification of the bases with dimethyl sulphate. The most striking result concerns C56, which becomes reactive in unmodified tRNAAsp, indicating the disruption of the C56-G19 base pair involved in the D- and T-loop interaction. The chemical data indicate that unmodified tRNAAsp transcripts possess a relaxed conformation compared to that of the native tRNA. This conclusion is confirmed by thermal melting experiments. Thus it can be proposed that post-transcriptional modifications of nucleotides in tRNA stabilize the biologically active conformations in these molecules.</abstract><subject><genre>Keywords</genre><topic>tRNAAsp transcripts</topic><topic>chemical RNA probes</topic><topic>thermal RNA melting</topic><topic>RNA conformation</topic><topic>modified nucleotides</topic></subject><subject><genre>Abbreviations</genre><topic>NTP : nucleoside triphosphate (N = A, G, U, C)</topic><topic>DTE : dithioerythritol</topic><topic>EDTA : ethylendiaminetetraacetic acid</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">1990</dateIssued></originInfo><identifier type="ISSN">0300-9084</identifier><identifier type="PII">S0300-9084(00)X0116-2</identifier><part><date>1990</date><detail type="volume"><number>72</number><caption>vol.</caption></detail><detail type="issue"><number>10</number><caption>no.</caption></detail><extent unit="issue-pages"><start>705</start><end>765</end></extent><extent unit="pages"><start>735</start><end>743</end></extent></part></relatedItem><identifier type="istex">87A0DD688E17D2C2BCD3003336CD37F4F786D175</identifier><identifier type="ark">ark:/67375/6H6-R6M7RKB8-V</identifier><identifier type="DOI">10.1016/0300-9084(90)90158-D</identifier><identifier type="PII">0300-9084(90)90158-D</identifier><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></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-R6M7RKB8-V/record.json</uri></json:item></metadata></istex></record>Pour manipuler ce document sous Unix (Dilib)
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