Measles Virus V Protein Binds Zinc
Identifieur interne : 001068 ( Istex/Corpus ); précédent : 001067; suivant : 001069Measles Virus V Protein Binds Zinc
Auteurs : Peter Liston ; Dalius J. BriedisSource :
- Virology [ 0042-6822 ] ; 1994.
Abstract
Abstract: Measles virus transcription generates multiple P/C gene-specific mRNAs by a process which has been termed editing. In one of these mRNAs, the cotranscriptional addition of a single nontemplated G residue allows translational access to the V protein reading frame. The protein translated from this mRNA has been called V and consists of 231 amino-terminal amino acid residues identical to those at the amino terminus of the P protein followed by a unique carboxy-terminal domain consisting of 68 amino acids from the V reading frame. The most striking feature of this unique domain is the presence within it of seven cysteine residues whose presence and position are highly conserved among different paramyxoviruses. The number and arrangement of these cysteine residues is suggestive of a zinc finger protein. We have used a zinc binding protocol to determine that V protein does indeed bind zinc, have further demonstrated that this metal binding activity is highly specific to zinc, and have shown that it is the unique carboxy-terminal domain of the V protein that is responsible for zinc binding.
Url:
DOI: 10.1006/viro.1994.1050
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Briedis</name><affiliation><mods:affiliation>Department of Microbiology and Immunology, McGill University, 3775 University Street, Montreal, Quebec H3A 2B4, Canada</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:45AB4C7C197E20A2849DFAE34BA12AFE089F4ACB</idno><date when="1994" year="1994">1994</date><idno type="doi">10.1006/viro.1994.1050</idno><idno type="url">https://api.istex.fr/ark:/67375/6H6-156K2JTT-5/fulltext.pdf</idno><idno type="wicri:Area/Istex/Corpus">001068</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">001068</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main" xml:lang="en">Measles Virus V Protein Binds Zinc</title><author><name sortKey="Liston, Peter" sort="Liston, Peter" uniqKey="Liston P" first="Peter" last="Liston">Peter Liston</name><affiliation><mods:affiliation>Department of Microbiology and Immunology, McGill University, 3775 University Street, Montreal, Quebec H3A 2B4, Canada</mods:affiliation></affiliation></author><author><name sortKey="Briedis, Dalius J" sort="Briedis, Dalius J" uniqKey="Briedis D" first="Dalius J." last="Briedis">Dalius J. Briedis</name><affiliation><mods:affiliation>Department of Microbiology and Immunology, McGill University, 3775 University Street, Montreal, Quebec H3A 2B4, Canada</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Virology</title><title level="j" type="abbrev">YVIRO</title><idno type="ISSN">0042-6822</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1994">1994</date><biblScope unit="volume">198</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="399">399</biblScope><biblScope unit="page" to="404">404</biblScope></imprint><idno type="ISSN">0042-6822</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0042-6822</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Measles virus transcription generates multiple P/C gene-specific mRNAs by a process which has been termed editing. In one of these mRNAs, the cotranscriptional addition of a single nontemplated G residue allows translational access to the V protein reading frame. The protein translated from this mRNA has been called V and consists of 231 amino-terminal amino acid residues identical to those at the amino terminus of the P protein followed by a unique carboxy-terminal domain consisting of 68 amino acids from the V reading frame. The most striking feature of this unique domain is the presence within it of seven cysteine residues whose presence and position are highly conserved among different paramyxoviruses. The number and arrangement of these cysteine residues is suggestive of a zinc finger protein. 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In one of these mRNAs, the cotranscriptional addition of a single nontemplated G residue allows translational access to the V protein reading frame. The protein translated from this mRNA has been called V and consists of 231 amino-terminal amino acid residues identical to those at the amino terminus of the P protein followed by a unique carboxy-terminal domain consisting of 68 amino acids from the V reading frame. The most striking feature of this unique domain is the presence within it of seven cysteine residues whose presence and position are highly conserved among different paramyxoviruses. The number and arrangement of these cysteine residues is suggestive of a zinc finger protein. We have used a zinc binding protocol to determine that V protein does indeed bind zinc, have further demonstrated that this metal binding activity is highly specific to zinc, and have shown that it is the unique carboxy-terminal domain of the V protein that is responsible for zinc binding.</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Measles Virus V Protein Binds Zinc</title></titleInfo><titleInfo type="alternative" lang="en" contentType="CDATA"><title>Measles Virus V Protein Binds Zinc</title></titleInfo><name type="personal"><namePart type="given">Peter</namePart><namePart type="family">Liston</namePart><affiliation>Department of Microbiology and Immunology, McGill University, 3775 University Street, Montreal, Quebec H3A 2B4, Canada</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Dalius J.</namePart><namePart type="family">Briedis</namePart><affiliation>Department of Microbiology and Immunology, McGill University, 3775 University Street, Montreal, Quebec H3A 2B4, Canada</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="brief-communication" displayLabel="Short communication" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-S9SX2MFS-0">brief-communication</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1994</dateIssued><copyrightDate encoding="w3cdtf">1994</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: Measles virus transcription generates multiple P/C gene-specific mRNAs by a process which has been termed editing. In one of these mRNAs, the cotranscriptional addition of a single nontemplated G residue allows translational access to the V protein reading frame. The protein translated from this mRNA has been called V and consists of 231 amino-terminal amino acid residues identical to those at the amino terminus of the P protein followed by a unique carboxy-terminal domain consisting of 68 amino acids from the V reading frame. The most striking feature of this unique domain is the presence within it of seven cysteine residues whose presence and position are highly conserved among different paramyxoviruses. The number and arrangement of these cysteine residues is suggestive of a zinc finger protein. 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