A novel open reading frame in tobacco mosaic virus genome coding for a putative small, positively charged protein
Identifieur interne : 001753 ( Istex/Corpus ); précédent : 001752; suivant : 001754A novel open reading frame in tobacco mosaic virus genome coding for a putative small, positively charged protein
Auteurs : S. Yu. Morozov ; O. N. Denisenko ; D. A. Zelenina ; O. N. Fedorkin ; A. G. Solovyev ; E. Maiss ; R. Casper ; J. G. AtabekovSource :
- 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
Links to Exploration step
ISTEX:0F853F11A62E6AE633D0180060B8AFEEC5185CA3Le document en format XML
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Atabekov</name><affiliation><mods:affiliation>Correspondence and reprints</mods:affiliation></affiliation><affiliation><mods:affiliation>Department of Virology and AN Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119899, Russia</mods:affiliation></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><istex><corpusName>elsevier</corpusName><keywords><teeft><json:string>genome</json:string><json:string>codon</json:string><json:string>reticulocyte</json:string><json:string>rna</json:string><json:string>genomic</json:string><json:string>ribosome</json:string><json:string>mutagenesis</json:string><json:string>clone</json:string><json:string>tobamovirus</json:string><json:string>complex formation</json:string><json:string>viral</json:string><json:string>complex assembly</json:string><json:string>tobacco mosaic virus</json:string><json:string>rabbit reticulocyte lysate</json:string><json:string>translation products</json:string><json:string>nucleotide sequence</json:string><json:string>cdna clone</json:string><json:string>rabbit reticulocyte lysates</json:string><json:string>mosaic</json:string><json:string>nucleotide</json:string><json:string>deletion mutagenesis</json:string><json:string>initiation codon</json:string><json:string>cowpea strain</json:string><json:string>green mosaic virus</json:string><json:string>termination codon</json:string><json:string>vector sequences</json:string><json:string>endogeneous products</json:string><json:string>transcript</json:string><json:string>transport protein</json:string><json:string>glycerol cushion</json:string><json:string>pairwise alignments</json:string><json:string>tomato mosaic virus</json:string><json:string>comparative analysis</json:string><json:string>coat protein</json:string><json:string>monocistronic transcripts</json:string><json:string>mottle mosaic virus</json:string><json:string>pvuii site</json:string><json:string>mottle virus</json:string><json:string>crude fractionation</json:string><json:string>similar position</json:string><json:string>major product</json:string><json:string>open reading frame</json:string><json:string>amino acids</json:string><json:string>molecular composition</json:string><json:string>viral rnas</json:string><json:string>subgenomic size</json:string><json:string>cellular protein</json:string><json:string>translation factors</json:string><json:string>complete nucleotide sequence</json:string><json:string>potato virus</json:string></teeft></keywords><author><json:item><name>S.Yu. Morozov</name><affiliations><json:string>Department of Virology and AN Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119899, Russia</json:string></affiliations></json:item><json:item><name>O.N. Denisenko</name><affiliations><json:string>Institute of Protein Research, Pushchino, Moscow region 142292, Russia</json:string></affiliations></json:item><json:item><name>D.A. Zelenina</name><affiliations><json:string>Institute of Microbiology, Russian Academy of Science, Moscow 117811, Russia</json:string></affiliations></json:item><json:item><name>O.N. Fedorkin</name><affiliations><json:string>Department of Virology and AN Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119899, Russia</json:string></affiliations></json:item><json:item><name>A.G. Solovyev</name><affiliations><json:string>Department of Virology and AN Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119899, Russia</json:string></affiliations></json:item><json:item><name>E. Maiss</name><affiliations><json:string>Institute of Biochemistry and Plant Virology, Biologische Bundesanstalt, Messeweg 11/12, D-3300, Braunschweig, Germany</json:string></affiliations></json:item><json:item><name>R. Casper</name><affiliations><json:string>Institute of Biochemistry and Plant Virology, Biologische Bundesanstalt, Messeweg 11/12, D-3300, Braunschweig, Germany</json:string></affiliations></json:item><json:item><name>J.G. Atabekov</name><affiliations><json:string>Correspondence and reprints</json:string><json:string>Department of Virology and AN Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119899, Russia</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>recombinant DNA</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>in vitro translation</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>plant virus</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>tobacco mosaic virus</value></json:item></subject><arkIstex>ark:/67375/6H6-G56QVT7P-J</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><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.</abstract><qualityIndicators><score>7.507</score><pdfWordCount>3695</pdfWordCount><pdfCharCount>23585</pdfCharCount><pdfVersion>1.2</pdfVersion><pdfPageCount>7</pdfPageCount><pdfPageSize>605 x 792 pts</pdfPageSize><refBibsNative>true</refBibsNative><abstractWordCount>151</abstractWordCount><abstractCharCount>1022</abstractCharCount><keywordCount>4</keywordCount></qualityIndicators><title>A novel open reading frame in tobacco mosaic virus genome coding for a putative small, positively charged protein</title><pmid><json:string>8286438</json:string></pmid><pii><json:string>0300-9084(93)90096-B</json:string></pii><genre><json:string>research-article</json:string></genre><serie><title>The Plant Viruses</title><language><json:string>unknown</json:string></language><volume>Vol 2</volume><pages><first>105</first><last>132</last></pages></serie><host><title>Biochimie</title><language><json:string>unknown</json:string></language><publicationDate>1993</publicationDate><issn><json:string>0300-9084</json:string></issn><pii><json:string>S0300-9084(00)X0149-6</json:string></pii><volume>75</volume><issue>8</issue><pages><first>659</first><last>665</last></pages><genre><json:string>journal</json:string></genre></host><namedEntities><unitex><date><json:string>1993</json:string></date><geogName></geogName><orgName><json:string>Protein Research, Pushchino, Moscow</json:string><json:string>According CO</json:string><json:string>Institute of Microbiology, Russian Academy of Science, Moscow</json:string></orgName><orgName_funder></orgName_funder><orgName_provider></orgName_provider><persName><json:string>B. 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xml:id="author-0000"><persName><forename type="first">S.Yu.</forename><surname>Morozov</surname></persName><affiliation>Department of Virology and AN Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119899, Russia</affiliation></author><author xml:id="author-0001"><persName><forename type="first">O.N.</forename><surname>Denisenko</surname></persName><affiliation>Institute of Protein Research, Pushchino, Moscow region 142292, Russia</affiliation></author><author xml:id="author-0002"><persName><forename type="first">D.A.</forename><surname>Zelenina</surname></persName><affiliation>Institute of Microbiology, Russian Academy of Science, Moscow 117811, Russia</affiliation></author><author xml:id="author-0003"><persName><forename type="first">O.N.</forename><surname>Fedorkin</surname></persName><affiliation>Department of Virology and AN Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119899, 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xml:lang="en"><p>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.</p></abstract><textClass><keywords scheme="keyword"><list><head>Keywords</head><item><term>recombinant DNA</term></item><item><term>in vitro translation</term></item><item><term>plant virus</term></item><item><term>tobacco mosaic virus</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1993">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-G56QVT7P-J/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>9390096B</aid><ce:pii>0300-9084(93)90096-B</ce:pii><ce:doi>10.1016/0300-9084(93)90096-B</ce:doi><ce:copyright type="unknown" year="1993"></ce:copyright></item-info><head><ce:title>A novel open reading frame in tobacco mosaic virus genome coding for a putative small, positively charged protein</ce:title><ce:author-group><ce:author><ce:given-name>S.Yu.</ce:given-name><ce:surname>Morozov</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>a</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>O.N.</ce:given-name><ce:surname>Denisenko</ce:surname><ce:cross-ref refid="AFF2"><ce:sup>b</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>D.A.</ce:given-name><ce:surname>Zelenina</ce:surname><ce:cross-ref refid="AFF3"><ce:sup>c</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>O.N.</ce:given-name><ce:surname>Fedorkin</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>a</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>A.G.</ce:given-name><ce:surname>Solovyev</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>a</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>E.</ce:given-name><ce:surname>Maiss</ce:surname><ce:cross-ref refid="AFF4"><ce:sup>d</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>R.</ce:given-name><ce:surname>Casper</ce:surname><ce:cross-ref refid="AFF4"><ce:sup>d</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>J.G.</ce:given-name><ce:surname>Atabekov</ce:surname><ce:cross-ref refid="COR1"><ce:sup>∗</ce:sup></ce:cross-ref><ce:cross-ref refid="AFF1"><ce:sup>a</ce:sup></ce:cross-ref></ce:author><ce:affiliation id="AFF1"><ce:label>a</ce:label><ce:textfn>Department of Virology and AN Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119899, Russia</ce:textfn></ce:affiliation><ce:affiliation id="AFF2"><ce:label>b</ce:label><ce:textfn>Institute of Protein Research, Pushchino, Moscow region 142292, Russia</ce:textfn></ce:affiliation><ce:affiliation id="AFF3"><ce:label>c</ce:label><ce:textfn>Institute of Microbiology, Russian Academy of Science, Moscow 117811, Russia</ce:textfn></ce:affiliation><ce:affiliation id="AFF4"><ce:label>d</ce:label><ce:textfn>Institute of Biochemistry and Plant Virology, Biologische Bundesanstalt, Messeweg 11/12, D-3300, Braunschweig, Germany</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="15" month="1" year="1993"></ce:date-received><ce:date-accepted day="3" month="2" year="1993"></ce:date-accepted><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>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. <ce:italic>In vitro</ce:italic> translation of the monocistronic artificial transcripts generated with T7 RNA polymerase yielded a protein of <ce:italic>M</ce:italic><ce:inf><ce:italic>r</ce:italic></ce:inf> 4000 (p4) and an unexpected trypsin-sensitive complex of <ce:italic>M</ce:italic><ce:inf><ce:italic>r</ce:italic></ce:inf> 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 <ce:italic>M</ce:italic><ce:inf><ce:italic>r</ce:italic></ce:inf> 50000 that is a component of the translation apparatus.</ce:simple-para></ce:abstract-sec></ce:abstract><ce:keywords><ce:section-title>Keywords</ce:section-title><ce:keyword><ce:text>recombinant DNA</ce:text></ce:keyword><ce:keyword><ce:text><ce:italic>in vitro</ce:italic> translation</ce:text></ce:keyword><ce:keyword><ce:text>plant virus</ce:text></ce:keyword><ce:keyword><ce:text>tobacco mosaic virus</ce:text></ce:keyword></ce:keywords></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>A novel open reading frame in tobacco mosaic virus genome coding for a putative small, positively charged protein</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>A novel open reading frame in tobacco mosaic virus genome coding for a putative small, positively charged protein</title></titleInfo><name type="personal"><namePart type="given">S.Yu.</namePart><namePart type="family">Morozov</namePart><affiliation>Department of Virology and AN Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119899, Russia</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">O.N.</namePart><namePart type="family">Denisenko</namePart><affiliation>Institute of Protein Research, Pushchino, Moscow region 142292, Russia</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">D.A.</namePart><namePart type="family">Zelenina</namePart><affiliation>Institute of Microbiology, Russian Academy of Science, Moscow 117811, Russia</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">O.N.</namePart><namePart type="family">Fedorkin</namePart><affiliation>Department of Virology and AN Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119899, Russia</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">A.G.</namePart><namePart type="family">Solovyev</namePart><affiliation>Department of Virology and AN Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119899, Russia</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">E.</namePart><namePart type="family">Maiss</namePart><affiliation>Institute of Biochemistry and Plant Virology, Biologische Bundesanstalt, Messeweg 11/12, D-3300, Braunschweig, Germany</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">R.</namePart><namePart type="family">Casper</namePart><affiliation>Institute of Biochemistry and Plant Virology, Biologische Bundesanstalt, Messeweg 11/12, D-3300, Braunschweig, Germany</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">J.G.</namePart><namePart type="family">Atabekov</namePart><affiliation>Correspondence and reprints</affiliation><affiliation>Department of Virology and AN Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119899, Russia</affiliation><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">1993</dateIssued><copyrightDate encoding="w3cdtf">1993</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract 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.</abstract><subject><genre>Keywords</genre><topic>recombinant DNA</topic><topic>in vitro translation</topic><topic>plant virus</topic><topic>tobacco mosaic virus</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">1993</dateIssued></originInfo><identifier type="ISSN">0300-9084</identifier><identifier type="PII">S0300-9084(00)X0149-6</identifier><part><date>1993</date><detail type="volume"><number>75</number><caption>vol.</caption></detail><detail type="issue"><number>8</number><caption>no.</caption></detail><extent unit="issue-pages"><start>635</start><end>755</end></extent><extent unit="pages"><start>659</start><end>665</end></extent></part></relatedItem><identifier type="istex">0F853F11A62E6AE633D0180060B8AFEEC5185CA3</identifier><identifier type="ark">ark:/67375/6H6-G56QVT7P-J</identifier><identifier type="DOI">10.1016/0300-9084(93)90096-B</identifier><identifier type="PII">0300-9084(93)90096-B</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-G56QVT7P-J/record.json</uri></json:item></metadata></istex></record>Pour manipuler ce document sous Unix (Dilib)
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