Tad1p, a yeast tRNA‐specific adenosine deaminase, is related to the mammalian pre‐mRNA editing enzymes ADAR1 and ADAR2
Identifieur interne : 000286 ( France/Analysis ); précédent : 000285; suivant : 000287Tad1p, a yeast tRNA‐specific adenosine deaminase, is related to the mammalian pre‐mRNA editing enzymes ADAR1 and ADAR2
Auteurs : André Gerber [Suisse] ; Henri Grosjean [France] ; Thorsten Melcher [Allemagne] ; Walter Keller [Suisse]Source :
- The EMBO Journal [ 0261-4189 ] ; 1998-08-17.
English descriptors
- Teeft :
- Adar, Adar enzyme family, Adar1, Adar2, Adenosine, Adenosine deaminase, Adenosine deaminase assay, Adenosine deaminases, Anticodon, Anticodon loop, Assay, Auxilien, Base pair, Biol, Chem, Clone, Coding sequence, Deaminase, Deaminase domain, Deaminases, Dsrbds, Dsrna, Editing, Editing activity, Editing enzymes, Editing enzymes adar1, Enzymatic formation, Enzyme, Eukaryotic, Eukaryotic trnaala, Genome, Inosine, Mammalian adars, Mrna, Mutant, Mutant cells, Mutant trnaala, Mutation, Natl acad, Nucleic acids, Plasmid, Primer, Promoter, Reaction mixture, Receptor, Recombinant, Recombinant protein, Recombinant tad1p, Red2, Saccharomyces cerevisiae, Sequence analysis, Subcloned, Tad1, Tad1 gene, Tad1p, Tad1p activity, Trna, Trna genes, Trna substrate, Trnaala, Trnaasp, Trp1, Trp1 gene, Trp1 marker, Unpublished results, Yeast, Yeast adenosine deaminase, Yeast protein, Yeast trnaala, Yeast trnaasp.
Abstract
We have identified an RNA‐specific adenosine deaminase (termed Tad1p/scADAT1) from Saccharomyces cerevisiae that selectively converts adenosine at position 37 of eukaryotic tRNAAla to inosine. The activity of purified recombinant Tad1p depends on the conformation of its tRNA substrate and the enzyme was found to be inactive on all other types of RNA tested. Mutant strains in which the TAD1 gene is disrupted are viable but lack Tad1p enzyme activity and their tRNAAla is not modified at position A37. Transformation of the mutant cells with the TAD1 gene restored enzyme activity. Tad1p has significant sequence similarity with the mammalian editing enzymes which act on specific precursor‐mRNAs and on long double‐stranded RNA. These findings suggest an evolutionary link between pre‐mRNA editing and tRNA modification.
Url:
DOI: 10.1093/emboj/17.16.4780
Affiliations:
- Allemagne, France, Suisse
- Bade-Wurtemberg, District de Karlsruhe, Île-de-France
- Gif‐sur‐Yvette, Heidelberg
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sort="Gerber, Andre" uniqKey="Gerber A" first="André" last="Gerber">André Gerber</name><affiliation wicri:level="1"><country xml:lang="fr">Suisse</country><wicri:regionArea>Department of Cell Biology, Biozentrum, University of Basel, CH‐4056, Basel</wicri:regionArea><wicri:noRegion>Basel</wicri:noRegion></affiliation></author><author><name sortKey="Grosjean, Henri" sort="Grosjean, Henri" uniqKey="Grosjean H" first="Henri" last="Grosjean">Henri Grosjean</name><affiliation wicri:level="3"><country xml:lang="fr">France</country><wicri:regionArea>Laboratory of Structural Enzymology and Biochemistry, CNRS, F‐91198, Gif‐sur‐Yvette</wicri:regionArea><placeName><region type="region" nuts="2">Île-de-France</region><settlement type="city">Gif‐sur‐Yvette</settlement></placeName></affiliation></author><author><name sortKey="Melcher, Thorsten" sort="Melcher, Thorsten" uniqKey="Melcher T" first="Thorsten" last="Melcher">Thorsten Melcher</name><affiliation wicri:level="3"><country 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type="ISSN">0261-4189</idno><idno type="eISSN">1460-2075</idno><imprint><biblScope unit="vol">17</biblScope><biblScope unit="issue">16</biblScope><biblScope unit="page" from="4780">4780</biblScope><biblScope unit="page" to="4789">4789</biblScope><biblScope unit="page-count">10</biblScope><publisher>John Wiley & Sons, Ltd</publisher><pubPlace>Chichester, UK</pubPlace><date type="published" when="1998-08-17">1998-08-17</date></imprint><idno type="ISSN">0261-4189</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0261-4189</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Adar</term><term>Adar enzyme family</term><term>Adar1</term><term>Adar2</term><term>Adenosine</term><term>Adenosine deaminase</term><term>Adenosine deaminase assay</term><term>Adenosine deaminases</term><term>Anticodon</term><term>Anticodon loop</term><term>Assay</term><term>Auxilien</term><term>Base pair</term><term>Biol</term><term>Chem</term><term>Clone</term><term>Coding sequence</term><term>Deaminase</term><term>Deaminase domain</term><term>Deaminases</term><term>Dsrbds</term><term>Dsrna</term><term>Editing</term><term>Editing activity</term><term>Editing enzymes</term><term>Editing enzymes adar1</term><term>Enzymatic formation</term><term>Enzyme</term><term>Eukaryotic</term><term>Eukaryotic trnaala</term><term>Genome</term><term>Inosine</term><term>Mammalian adars</term><term>Mrna</term><term>Mutant</term><term>Mutant cells</term><term>Mutant trnaala</term><term>Mutation</term><term>Natl acad</term><term>Nucleic acids</term><term>Plasmid</term><term>Primer</term><term>Promoter</term><term>Reaction mixture</term><term>Receptor</term><term>Recombinant</term><term>Recombinant protein</term><term>Recombinant tad1p</term><term>Red2</term><term>Saccharomyces cerevisiae</term><term>Sequence analysis</term><term>Subcloned</term><term>Tad1</term><term>Tad1 gene</term><term>Tad1p</term><term>Tad1p activity</term><term>Trna</term><term>Trna genes</term><term>Trna substrate</term><term>Trnaala</term><term>Trnaasp</term><term>Trp1</term><term>Trp1 gene</term><term>Trp1 marker</term><term>Unpublished results</term><term>Yeast</term><term>Yeast adenosine deaminase</term><term>Yeast protein</term><term>Yeast trnaala</term><term>Yeast trnaasp</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract">We have identified an RNA‐specific adenosine deaminase (termed Tad1p/scADAT1) from Saccharomyces cerevisiae that selectively converts adenosine at position 37 of eukaryotic tRNAAla to inosine. The activity of purified recombinant Tad1p depends on the conformation of its tRNA substrate and the enzyme was found to be inactive on all other types of RNA tested. Mutant strains in which the TAD1 gene is disrupted are viable but lack Tad1p enzyme activity and their tRNAAla is not modified at position A37. Transformation of the mutant cells with the TAD1 gene restored enzyme activity. Tad1p has significant sequence similarity with the mammalian editing enzymes which act on specific precursor‐mRNAs and on long double‐stranded RNA. These findings suggest an evolutionary link between pre‐mRNA editing and tRNA modification.</div></front></TEI><affiliations><list><country><li>Allemagne</li><li>France</li><li>Suisse</li></country><region><li>Bade-Wurtemberg</li><li>District de Karlsruhe</li><li>Île-de-France</li></region><settlement><li>Gif‐sur‐Yvette</li><li>Heidelberg</li></settlement></list><tree><country name="Suisse"><noRegion><name sortKey="Gerber, Andre" sort="Gerber, Andre" uniqKey="Gerber A" first="André" last="Gerber">André Gerber</name></noRegion><name sortKey="Keller, Walter" sort="Keller, Walter" uniqKey="Keller W" first="Walter" last="Keller">Walter Keller</name><name sortKey="Keller, Walter" sort="Keller, Walter" uniqKey="Keller W" first="Walter" last="Keller">Walter Keller</name></country><country name="France"><region name="Île-de-France"><name sortKey="Grosjean, Henri" sort="Grosjean, Henri" uniqKey="Grosjean H" first="Henri" last="Grosjean">Henri Grosjean</name></region></country><country name="Allemagne"><region name="Bade-Wurtemberg"><name sortKey="Melcher, Thorsten" sort="Melcher, Thorsten" uniqKey="Melcher T" first="Thorsten" last="Melcher">Thorsten Melcher</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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