A novel open reading frame in tobacco mosaic virus genome coding for a putative small, positively charged protein
Identifieur interne : 004599 ( Main/Exploration ); précédent : 004598; suivant : 004600A novel open reading frame in tobacco mosaic virus genome coding for a putative small, positively charged protein
Auteurs : S. Yu. Morozov [Russie] ; O. N. Denisenko [Russie] ; D. A. Zelenina [Russie] ; O. N. Fedorkin [Russie] ; A. G. Solovyev [Russie] ; E. Maiss [Allemagne] ; R. Casper [Allemagne] ; J. G. Atabekov [Russie]Source :
- Biochimie [ 0300-9084 ] ; 1993.
English descriptors
- Teeft :
- Amino acids, Cdna clone, Cellular protein, Clone, Coat protein, Codon, Comparative analysis, Complete nucleotide sequence, Complex assembly, Complex formation, Cowpea strain, Crude fractionation, Deletion mutagenesis, Endogeneous products, Genome, Genomic, Glycerol cushion, Green mosaic virus, Initiation codon, Major product, Molecular composition, Monocistronic transcripts, Mosaic, Mottle mosaic virus, Mottle virus, Mutagenesis, Nucleotide, Nucleotide sequence, Open reading frame, Pairwise alignments, Potato virus, Pvuii site, Rabbit reticulocyte lysate, Rabbit reticulocyte lysates, Reticulocyte, Ribosome, Rna, Similar position, Subgenomic size, Termination codon, Tobacco mosaic virus, Tobamovirus, Tomato mosaic virus, Transcript, Translation factors, Translation products, Transport protein, Vector sequences, Viral, Viral rnas.
Abstract
Abstract: From sequence comparisons between the tobamovirus genomes an open reading frame (ORF-X) potentially encoding a small, positively charged protein (33- to 45-amino-acids long) was found to overlap the immediate 3′ and 5′ sides of the transport protein gene and coat protein gene, respectively. In vitro translation of the monocistronic artificial transcripts generated with T7 RNA polymerase yielded a protein of Mr 4000 (p4) and an unexpected trypsin-sensitive complex of Mr 54000 that was resistant to reduction with 2-mercaptoethanol but could be dissociated by 8 M urea. Assembly of this complex was inhibited completely by site-directed mutagenesis within a conserved, positively charged 5-amino-acid long segment of the ORF-X protein. After centrifugation in low salt buffer the 54-kDa complex remained mostly associated with ribosomes. Apparently this complex represents a specific aggregate of the p4 product of ORF-X with a protein of approximate Mr 50000 that is a component of the translation apparatus.
Url:
DOI: 10.1016/0300-9084(93)90096-B
Affiliations:
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Solovyev</name><affiliation wicri:level="4"><country xml:lang="fr">Russie</country><wicri:regionArea>Department of Virology and AN Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119899</wicri:regionArea><placeName><settlement type="city">Moscou</settlement><region>District fédéral central</region></placeName><orgName type="university">Université d'État de Moscou</orgName><placeName><settlement type="city">Moscou</settlement><region>District fédéral central</region></placeName></affiliation></author><author><name sortKey="Maiss, E" sort="Maiss, E" uniqKey="Maiss E" first="E." last="Maiss">E. 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Atabekov</name><affiliation></affiliation><affiliation wicri:level="4"><country xml:lang="fr">Russie</country><wicri:regionArea>Department of Virology and AN Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119899</wicri:regionArea><placeName><settlement type="city">Moscou</settlement><region>District fédéral central</region></placeName><orgName type="university">Université d'État de Moscou</orgName><placeName><settlement type="city">Moscou</settlement><region>District fédéral central</region></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="1993">1993</date><biblScope unit="volume">75</biblScope><biblScope unit="issue">8</biblScope><biblScope unit="page" from="659">659</biblScope><biblScope unit="page" to="665">665</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>Amino acids</term><term>Cdna clone</term><term>Cellular protein</term><term>Clone</term><term>Coat protein</term><term>Codon</term><term>Comparative analysis</term><term>Complete nucleotide sequence</term><term>Complex assembly</term><term>Complex formation</term><term>Cowpea strain</term><term>Crude fractionation</term><term>Deletion mutagenesis</term><term>Endogeneous products</term><term>Genome</term><term>Genomic</term><term>Glycerol cushion</term><term>Green mosaic virus</term><term>Initiation codon</term><term>Major product</term><term>Molecular composition</term><term>Monocistronic transcripts</term><term>Mosaic</term><term>Mottle mosaic virus</term><term>Mottle virus</term><term>Mutagenesis</term><term>Nucleotide</term><term>Nucleotide sequence</term><term>Open reading frame</term><term>Pairwise alignments</term><term>Potato virus</term><term>Pvuii site</term><term>Rabbit reticulocyte lysate</term><term>Rabbit reticulocyte lysates</term><term>Reticulocyte</term><term>Ribosome</term><term>Rna</term><term>Similar position</term><term>Subgenomic size</term><term>Termination codon</term><term>Tobacco mosaic virus</term><term>Tobamovirus</term><term>Tomato mosaic virus</term><term>Transcript</term><term>Translation factors</term><term>Translation products</term><term>Transport protein</term><term>Vector sequences</term><term>Viral</term><term>Viral rnas</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: From sequence comparisons between the tobamovirus genomes an open reading frame (ORF-X) potentially encoding a small, positively charged protein (33- to 45-amino-acids long) was found to overlap the immediate 3′ and 5′ sides of the transport protein gene and coat protein gene, respectively. In vitro translation of the monocistronic artificial transcripts generated with T7 RNA polymerase yielded a protein of Mr 4000 (p4) and an unexpected trypsin-sensitive complex of Mr 54000 that was resistant to reduction with 2-mercaptoethanol but could be dissociated by 8 M urea. Assembly of this complex was inhibited completely by site-directed mutagenesis within a conserved, positively charged 5-amino-acid long segment of the ORF-X protein. After centrifugation in low salt buffer the 54-kDa complex remained mostly associated with ribosomes. Apparently this complex represents a specific aggregate of the p4 product of ORF-X with a protein of approximate Mr 50000 that is a component of the translation apparatus.</div></front></TEI><affiliations><list><country><li>Allemagne</li><li>Russie</li></country><region><li>District fédéral central</li></region><settlement><li>Moscou</li></settlement><orgName><li>Université d'État de Moscou</li></orgName></list><tree><country name="Russie"><region name="District fédéral central"><name sortKey="Morozov, S Yu" sort="Morozov, S Yu" uniqKey="Morozov S" first="S. Yu." last="Morozov">S. Yu. Morozov</name></region><name sortKey="Atabekov, J G" sort="Atabekov, J G" uniqKey="Atabekov J" first="J. G." last="Atabekov">J. G. Atabekov</name><name sortKey="Denisenko, O N" sort="Denisenko, O N" uniqKey="Denisenko O" first="O. N." last="Denisenko">O. N. Denisenko</name><name sortKey="Fedorkin, O N" sort="Fedorkin, O N" uniqKey="Fedorkin O" first="O. N." last="Fedorkin">O. N. Fedorkin</name><name sortKey="Solovyev, A G" sort="Solovyev, A G" uniqKey="Solovyev A" first="A. G." last="Solovyev">A. G. Solovyev</name><name sortKey="Zelenina, D A" sort="Zelenina, D A" uniqKey="Zelenina D" first="D. A." last="Zelenina">D. A. Zelenina</name></country><country name="Allemagne"><noRegion><name sortKey="Maiss, E" sort="Maiss, E" uniqKey="Maiss E" first="E." last="Maiss">E. Maiss</name></noRegion><name sortKey="Casper, R" sort="Casper, R" uniqKey="Casper R" first="R." last="Casper">R. Casper</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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