Conformation in solution of yeast tRNAAsp transcripts deprived of modified nucleotides
Identifieur interne : 000393 ( France/Analysis ); précédent : 000392; suivant : 000394Conformation in solution of yeast tRNAAsp transcripts deprived of modified nucleotides
Auteurs : V. Perret [France] ; A. Garcia [France] ; J. Puglisi [France] ; H. Grosjean [France] ; J. P. Ebel [France] ; C. Florentz [France] ; R. Giegé [France]Source :
- 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
Affiliations:
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ISTEX:87A0DD688E17D2C2BCD3003336CD37F4F786D175Le document en format XML
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Grosjean</name><affiliation wicri:level="3"><country xml:lang="fr">France</country><wicri:regionArea>Laboratoire de Biochimie, Institut de Biologie Moléculaire et Cellulaire, Centre National de la Recherche Scientifique 15, rue René Descartes, F-67084 Strasbourg Cedex</wicri:regionArea><placeName><region type="region" nuts="2">Grand Est</region><region type="old region" nuts="2">Alsace (région administrative)</region><settlement type="city">Strasbourg</settlement></placeName></affiliation></author><author><name sortKey="Ebel, J P" sort="Ebel, J P" uniqKey="Ebel J" first="J. P." last="Ebel">J. P. Ebel</name><affiliation wicri:level="3"><country xml:lang="fr">France</country><wicri:regionArea>Laboratoire de Biochimie, Institut de Biologie Moléculaire et Cellulaire, Centre National de la Recherche Scientifique 15, rue René Descartes, F-67084 Strasbourg Cedex</wicri:regionArea><placeName><region type="region" nuts="2">Grand Est</region><region type="old region" nuts="2">Alsace (région administrative)</region><settlement type="city">Strasbourg</settlement></placeName></affiliation></author><author><name sortKey="Florentz, C" sort="Florentz, C" uniqKey="Florentz C" first="C." last="Florentz">C. 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Giegé</name><affiliation wicri:level="3"><country xml:lang="fr">France</country><wicri:regionArea>Laboratoire de Biochimie, Institut de Biologie Moléculaire et Cellulaire, Centre National de la Recherche Scientifique 15, rue René Descartes, F-67084 Strasbourg Cedex</wicri:regionArea><placeName><region type="region" nuts="2">Grand Est</region><region type="old region" nuts="2">Alsace (région administrative)</region><settlement type="city">Strasbourg</settlement></placeName></affiliation></author></analytic><monogr></monogr><series><title level="j">Biochimie</title><title level="j" type="abbrev">BIOCHI</title><idno type="ISSN">0300-9084</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1990">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><idno type="ISSN">0300-9084</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0300-9084</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Active conformations</term><term>Alkaline hydrolysis ladders</term><term>Aminoacylation</term><term>Base pair</term><term>Biol</term><term>Biol chem</term><term>Bold characters</term><term>Chemical probes</term><term>Cleavage</term><term>Cleavage experiments</term><term>Comparative chemical mapping</term><term>Comparative experiments</term><term>Conformation</term><term>Conformational</term><term>Conformational change</term><term>Conformational changes</term><term>Denaturing conditions</term><term>Diethyl pyrocarbonate</term><term>Dimethyl</term><term>Dimethyl sulphate</term><term>Ebel</term><term>Escherichia coli</term><term>Functional implications</term><term>Gieg6</term><term>Incorrect aminoacylations</term><term>Modification</term><term>Molecule</term><term>Moras</term><term>Native conditions</term><term>Native trna</term><term>Native trnaasp</term><term>Nucleic acids</term><term>Nucleotide</term><term>Oligonucleotides</term><term>Polymerase</term><term>Polynucleotide kinase</term><term>Proc natl acad</term><term>Promoter extension</term><term>Recherche scientifique</term><term>Sodium cacodylate</term><term>Structural mapping</term><term>Structural plasticity</term><term>Sulphate</term><term>Synthetase</term><term>Synthetic gene</term><term>Synthetic genes</term><term>Tertiary structure</term><term>Thermal stability</term><term>Transcript</term><term>Transcription</term><term>Transcriptional medium</term><term>Trna</term><term>Trna genes</term><term>Trna sequence</term><term>Trnaasp</term><term>Trnaasp molecules</term><term>Unmodified</term><term>Unmodified molecules</term><term>Unmodified transcript</term><term>Unmodified transcripts</term><term>Unmodified trnaasp</term><term>Unmodified trnaasp transcripts</term><term>Unmodified trnas</term><term>Yeast</term><term>Yeast phenylalanine transfer</term><term>Yeast trna</term><term>Yeast trnaasp</term><term>Yeast trnaasp transcripts</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml: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.</div></front></TEI><affiliations><list><country><li>France</li></country><region><li>Alsace (région administrative)</li><li>Grand Est</li></region><settlement><li>Strasbourg</li></settlement></list><tree><country name="France"><region name="Grand Est"><name sortKey="Perret, V" sort="Perret, V" uniqKey="Perret V" first="V." last="Perret">V. Perret</name></region><name sortKey="Ebel, J P" sort="Ebel, J P" uniqKey="Ebel J" first="J. P." last="Ebel">J. P. Ebel</name><name sortKey="Florentz, C" sort="Florentz, C" uniqKey="Florentz C" first="C." last="Florentz">C. Florentz</name><name sortKey="Garcia, A" sort="Garcia, A" uniqKey="Garcia A" first="A." last="Garcia">A. Garcia</name><name sortKey="Giege, R" sort="Giege, R" uniqKey="Giege R" first="R." last="Giegé">R. Giegé</name><name sortKey="Grosjean, H" sort="Grosjean, H" uniqKey="Grosjean H" first="H." last="Grosjean">H. Grosjean</name><name sortKey="Puglisi, J" sort="Puglisi, J" uniqKey="Puglisi J" first="J." last="Puglisi">J. Puglisi</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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