Organization of the sindbis virus nucleocapsid as revealed by bifunctional cross-linking agents
Identifieur interne : 000818 ( Istex/Corpus ); précédent : 000817; suivant : 000819Organization of the sindbis virus nucleocapsid as revealed by bifunctional cross-linking agents
Auteurs : Kevin Coombs ; Dennis T. BrownSource :
- Journal of Molecular Biology [ 0022-2836 ] ; 1987.
English descriptors
- Teeft :
- Academic press, Acheson tamm, Adjacent arrays, Adjacent capsid proteins, Adjacent proteins, Available lysine residues, Axis length, Bifunctional agent, Biol, Bsocoes, Buffer system, Capsid, Capsid protein, Capsid proteins, Caspar klug, Cell research institute, Concentration gradient, Densitometric scans, Different nucleocapsids, Dimer, Dimeric, Dimeric species, Dimethyl, Dimethyl pimelimidate, Dimethyl suberimidate, Disuccinimidyl tartarate, Effective bridge span size, Electron microscope, Electrophoresis sample buffer, Empty shells, Envelope proteins, Ethylene succinate, Fetal calf serum, Free capsid protein, Garoff simons, Glutaraldehyde, Greatest number, Harrison, Hexameric, Hexameric array, Hexameric arrays, High concentrations, Icosahedron, Imido esters, Intact nucleocapsids, Intact particles, Intact sindbis virus, Intact virions, Large number, Larger agents, Lower concentrations, Lysine, Lysine residues, Lysozyme, Major proteins, Mccarthy harrison, Molecular weights, Morphological alterations, Morphology, Nucleocapsid, Nucleocapsid shell, Nucleocapsid structure, Nucleocapsid surface, Nucleocapsids, Oligomers, Other agents, Pentameric, Pentameric aggregates, Pentameric array, Positive stain, Post infection, Previous investigators, Protein, Reagent, Regular icosahedron, Resolvable, Resolvable oligomers, Resolvable products, Resolvable species, Rice strauss, Rnase, Sample buffer, Silver stain, Similar ratios, Similar results, Sindbis, Sindbis nucleocapsid, Sindbis virus, Sindbis virus nucleocapsid, Sindbis virus nucleocapsids, Single array, Single protein, Soderlund, Sodium dodecyl sulfate, Span sizes, Spherical structure, Spike, Strauss, Sucrose gradients, Tail spike protein, Tail spike trimers, Total number, Triangulation number, Trimer, Trimeric, Trimeric aggregates, Trimeric array, Trimeric arrays, Unpublished results, Uranyl acetate, Various agents, Various concentrations, Various products, Various types, Virus envelope, Vonbonsdorff harrison, Wang richards.
Abstract
Abstract: Purified Sindbis virus nucleocapsids were reacted with a variety of bifunctional proteinspecific cross-linking agents. The products were analyzed in concentration-gradient polyacrylamide gels and amounts of various products determined. These studies indicated that available lysine residues within adjacent capsid proteins in purified intact nucleocapsids are separated by 6 Å. The capsid proteins in intact nucleocapsids are crosslinked in a pattern predicted for discrete monomeric entities, rather than in dimeric or trimeric aggregates. Purified, soluble capsid protein exists in a conformation that differs from the arrangement of protein within nucleocapsids. These conformational differences suggest that topological changes may occur in the capsid protein during virus maturation. Cross-linked nucleocapsids that were treated with RNases resulted in the generation of RNA-free protein shells that retained hexagonal morphology, indicating that, together, the RNA and protein form the outer surface of the nucleocapsid. These data are used to produce a model of the Sindbis virus nucleocapsid in which the proteins are arranged quasiequivalently in a T = 4 icosahedral shell.
Url:
DOI: 10.1016/0022-2836(87)90657-7
Links to Exploration step
ISTEX:1C03404FFB79D1D6E5A959D001D672FCA99662C5Le document en format XML
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Brown</name><affiliation><mods:affiliation>The Cell Research Institute and Department of Microbiology The University of Texas at Austin, Austin, TX 78713, U.S.A.</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Journal of Molecular Biology</title><title level="j" type="abbrev">YJMBI</title><idno type="ISSN">0022-2836</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1987">1987</date><biblScope unit="volume">195</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="359">359</biblScope><biblScope unit="page" to="371">371</biblScope></imprint><idno type="ISSN">0022-2836</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0022-2836</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Academic press</term><term>Acheson tamm</term><term>Adjacent arrays</term><term>Adjacent capsid proteins</term><term>Adjacent proteins</term><term>Available lysine residues</term><term>Axis length</term><term>Bifunctional agent</term><term>Biol</term><term>Bsocoes</term><term>Buffer system</term><term>Capsid</term><term>Capsid protein</term><term>Capsid proteins</term><term>Caspar klug</term><term>Cell research institute</term><term>Concentration gradient</term><term>Densitometric scans</term><term>Different nucleocapsids</term><term>Dimer</term><term>Dimeric</term><term>Dimeric species</term><term>Dimethyl</term><term>Dimethyl pimelimidate</term><term>Dimethyl suberimidate</term><term>Disuccinimidyl tartarate</term><term>Effective bridge span size</term><term>Electron microscope</term><term>Electrophoresis sample buffer</term><term>Empty shells</term><term>Envelope proteins</term><term>Ethylene succinate</term><term>Fetal calf serum</term><term>Free capsid protein</term><term>Garoff simons</term><term>Glutaraldehyde</term><term>Greatest number</term><term>Harrison</term><term>Hexameric</term><term>Hexameric array</term><term>Hexameric arrays</term><term>High concentrations</term><term>Icosahedron</term><term>Imido esters</term><term>Intact nucleocapsids</term><term>Intact particles</term><term>Intact sindbis virus</term><term>Intact virions</term><term>Large number</term><term>Larger agents</term><term>Lower concentrations</term><term>Lysine</term><term>Lysine residues</term><term>Lysozyme</term><term>Major proteins</term><term>Mccarthy harrison</term><term>Molecular weights</term><term>Morphological alterations</term><term>Morphology</term><term>Nucleocapsid</term><term>Nucleocapsid shell</term><term>Nucleocapsid structure</term><term>Nucleocapsid surface</term><term>Nucleocapsids</term><term>Oligomers</term><term>Other agents</term><term>Pentameric</term><term>Pentameric aggregates</term><term>Pentameric array</term><term>Positive stain</term><term>Post infection</term><term>Previous investigators</term><term>Protein</term><term>Reagent</term><term>Regular icosahedron</term><term>Resolvable</term><term>Resolvable oligomers</term><term>Resolvable products</term><term>Resolvable species</term><term>Rice strauss</term><term>Rnase</term><term>Sample buffer</term><term>Silver stain</term><term>Similar ratios</term><term>Similar results</term><term>Sindbis</term><term>Sindbis nucleocapsid</term><term>Sindbis virus</term><term>Sindbis virus nucleocapsid</term><term>Sindbis virus nucleocapsids</term><term>Single array</term><term>Single protein</term><term>Soderlund</term><term>Sodium dodecyl sulfate</term><term>Span sizes</term><term>Spherical structure</term><term>Spike</term><term>Strauss</term><term>Sucrose gradients</term><term>Tail spike protein</term><term>Tail spike trimers</term><term>Total number</term><term>Triangulation number</term><term>Trimer</term><term>Trimeric</term><term>Trimeric aggregates</term><term>Trimeric array</term><term>Trimeric arrays</term><term>Unpublished results</term><term>Uranyl acetate</term><term>Various agents</term><term>Various concentrations</term><term>Various products</term><term>Various types</term><term>Virus envelope</term><term>Vonbonsdorff harrison</term><term>Wang richards</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Purified Sindbis virus nucleocapsids were reacted with a variety of bifunctional proteinspecific cross-linking agents. The products were analyzed in concentration-gradient polyacrylamide gels and amounts of various products determined. These studies indicated that available lysine residues within adjacent capsid proteins in purified intact nucleocapsids are separated by 6 Å. The capsid proteins in intact nucleocapsids are crosslinked in a pattern predicted for discrete monomeric entities, rather than in dimeric or trimeric aggregates. Purified, soluble capsid protein exists in a conformation that differs from the arrangement of protein within nucleocapsids. These conformational differences suggest that topological changes may occur in the capsid protein during virus maturation. Cross-linked nucleocapsids that were treated with RNases resulted in the generation of RNA-free protein shells that retained hexagonal morphology, indicating that, together, the RNA and protein form the outer surface of the nucleocapsid. These data are used to produce a model of the Sindbis virus nucleocapsid in which the proteins are arranged quasiequivalently in a T = 4 icosahedral shell.</div></front></TEI><istex><corpusName>elsevier</corpusName><keywords><teeft><json:string>nucleocapsids</json:string><json:string>capsid</json:string><json:string>nucleocapsid</json:string><json:string>sindbis</json:string><json:string>capsid protein</json:string><json:string>trimer</json:string><json:string>dimeric</json:string><json:string>trimeric</json:string><json:string>dimer</json:string><json:string>resolvable</json:string><json:string>glutaraldehyde</json:string><json:string>intact nucleocapsids</json:string><json:string>rice strauss</json:string><json:string>envelope proteins</json:string><json:string>bsocoes</json:string><json:string>icosahedron</json:string><json:string>biol</json:string><json:string>lysine</json:string><json:string>hexameric</json:string><json:string>unpublished results</json:string><json:string>capsid 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proteins</json:string><json:string>sindbis nucleocapsid</json:string><json:string>silver stain</json:string><json:string>intact particles</json:string><json:string>wang richards</json:string><json:string>nucleocapsid shell</json:string><json:string>total number</json:string><json:string>imido esters</json:string><json:string>single array</json:string><json:string>adjacent arrays</json:string><json:string>vonbonsdorff harrison</json:string><json:string>sindbis virus</json:string><json:string>densitometric scans</json:string><json:string>nucleocapsid surface</json:string><json:string>cell research institute</json:string><json:string>resolvable oligomers</json:string><json:string>similar ratios</json:string><json:string>dimeric species</json:string><json:string>various types</json:string><json:string>span sizes</json:string><json:string>trimeric array</json:string><json:string>larger agents</json:string><json:string>bifunctional agent</json:string><json:string>electrophoresis sample buffer</json:string><json:string>hexameric array</json:string><json:string>regular icosahedron</json:string><json:string>single protein</json:string><json:string>positive stain</json:string><json:string>intact sindbis virus</json:string></teeft></keywords><author><json:item><name>Kevin Coombs</name><affiliations><json:string>The Cell Research Institute and Department of Microbiology The University of Texas at Austin, Austin, TX 78713, U.S.A.</json:string></affiliations></json:item><json:item><name>Dennis T. Brown</name><affiliations><json:string>The Cell Research Institute and Department of Microbiology The University of Texas at Austin, Austin, TX 78713, U.S.A.</json:string></affiliations></json:item></author><arkIstex>ark:/67375/6H6-BRMPHTV3-T</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>Abstract: Purified Sindbis virus nucleocapsids were reacted with a variety of bifunctional proteinspecific cross-linking agents. The products were analyzed in concentration-gradient polyacrylamide gels and amounts of various products determined. These studies indicated that available lysine residues within adjacent capsid proteins in purified intact nucleocapsids are separated by 6 Å. The capsid proteins in intact nucleocapsids are crosslinked in a pattern predicted for discrete monomeric entities, rather than in dimeric or trimeric aggregates. Purified, soluble capsid protein exists in a conformation that differs from the arrangement of protein within nucleocapsids. These conformational differences suggest that topological changes may occur in the capsid protein during virus maturation. Cross-linked nucleocapsids that were treated with RNases resulted in the generation of RNA-free protein shells that retained hexagonal morphology, indicating that, together, the RNA and protein form the outer surface of the nucleocapsid. These data are used to produce a model of the Sindbis virus nucleocapsid in which the proteins are arranged quasiequivalently in a T = 4 icosahedral shell.</abstract><qualityIndicators><score>8.98</score><pdfWordCount>5584</pdfWordCount><pdfCharCount>43438</pdfCharCount><pdfVersion>1.3</pdfVersion><pdfPageCount>13</pdfPageCount><pdfPageSize>576 x 828 pts</pdfPageSize><refBibsNative>true</refBibsNative><abstractWordCount>165</abstractWordCount><abstractCharCount>1192</abstractCharCount><keywordCount>0</keywordCount></qualityIndicators><title>Organization of the sindbis virus nucleocapsid as revealed by bifunctional cross-linking agents</title><pmid><json:string>3656418</json:string></pmid><pii><json:string>0022-2836(87)90657-7</json:string></pii><genre><json:string>research-article</json:string></genre><host><title>Journal of Molecular Biology</title><language><json:string>unknown</json:string></language><publicationDate>1987</publicationDate><issn><json:string>0022-2836</json:string></issn><pii><json:string>S0022-2836(00)X1131-X</json:string></pii><volume>195</volume><issue>2</issue><pages><first>359</first><last>371</last></pages><genre><json:string>journal</json:string></genre></host><namedEntities><unitex><date><json:string>1987</json:string><json:string>35S</json:string></date><geogName><json:string>Semliki</json:string></geogName><orgName><json:string>Brown The Cell Research Institute and Department of Microbiology The University of Texas</json:string><json:string>Pierce Chemical Company</json:string><json:string>Cell Research Institute</json:string><json:string>National Institutes of Health</json:string><json:string>Welch Foundation</json:string><json:string>Academic Press Inc.</json:string><json:string>Public Health Service</json:string></orgName><orgName_funder><json:string>Public Health Service</json:string></orgName_funder><orgName_provider></orgName_provider><persName><json:string>K. Coombs</json:string><json:string>Dennis</json:string><json:string>M. Hee-Yu</json:string><json:string>Jonathan King</json:string><json:string>J. King</json:string><json:string>Dr Kuan</json:string><json:string>D. T. Brown</json:string><json:string>Kevin Coombs</json:string></persName><placeName><json:string>TX</json:string><json:string>Rochester</json:string><json:string>NY</json:string><json:string>Austin</json:string></placeName><ref_url></ref_url><ref_bibl><json:string>Eagle, 1959</json:string><json:string>Abdella et al., 1979</json:string><json:string>Peacock & Dmgman, 1968</json:string><json:string>Manning et al., 1976</json:string><json:string>Hopwood, 1968</json:string><json:string>Smith & Brown, 1977</json:string><json:string>Rice & Strauss, 1982</json:string><json:string>Hajdu et al., 1979</json:string><json:string>Losso et al., 1986</json:string><json:string>Harrison, 1983</json:string><json:string>Soderlund et al., 1979</json:string><json:string>Soderlund, 1973</json:string><json:string>Brown, 1980</json:string><json:string>Murphy, 1980</json:string><json:string>Coombs et al., 1984</json:string><json:string>Richards & Knowles, 1968</json:string><json:string>Reissig & Orrell, 1970</json:string><json:string>those participating in the formation of vertices having 5-fold rotational symmetry and those forming the g-fold rotational arrays of the edges and faces of an icosahedron (Caspar & Klug, 1962</json:string><json:string>Strauss et al., 1968</json:string><json:string>Garoff & Simons, 1974</json:string><json:string>Helenius & Soderlund, 1973</json:string><json:string>Hardy et al., 1969</json:string><json:string>Coggins et al., 1976</json:string><json:string>Bonner & Laskey, 1974</json:string><json:string>Goldenberg et al., 1982</json:string><json:string>McCarthy & Harrison, 1977</json:string><json:string>vonBonsdorff t Harrison, 1975</json:string><json:string>Zarling et al., 1980</json:string><json:string>Scheefers et al., 1980</json:string><json:string>Wang & Richards, 1975</json:string><json:string>Samuelson & Kaesberg, 1970</json:string><json:string>Chamberlain, 1979</json:string><json:string>Hordern et al., 1979</json:string><json:string>Lutter et al., 1972</json:string><json:string>Acheson & Tamm, 1970</json:string><json:string>as described by (Jaspar & Klug, 1962</json:string></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/6H6-BRMPHTV3-T</json:string></ark><categories><wos><json:string>1 - science</json:string><json:string>2 - biochemistry & molecular biology</json:string></wos><scienceMetrix><json:string>1 - health sciences</json:string><json:string>2 - biomedical research</json:string><json:string>3 - biochemistry & molecular biology</json:string></scienceMetrix><scopus><json:string>1 - Life Sciences</json:string><json:string>2 - Biochemistry, Genetics and Molecular Biology</json:string><json:string>3 - Molecular Biology</json:string></scopus><inist><json:string>1 - sciences appliquees, technologies et medecines</json:string><json:string>2 - sciences biologiques et medicales</json:string><json:string>3 - sciences biologiques fondamentales et appliquees. psychologie</json:string></inist></categories><publicationDate>1987</publicationDate><copyrightDate>1987</copyrightDate><doi><json:string>10.1016/0022-2836(87)90657-7</json:string></doi><id>1C03404FFB79D1D6E5A959D001D672FCA99662C5</id><score>1</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-BRMPHTV3-T/fulltext.pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-BRMPHTV3-T/bundle.zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/ark:/67375/6H6-BRMPHTV3-T/fulltext.tei"><teiHeader><fileDesc><titleStmt><title level="a">Organization of the sindbis virus nucleocapsid as revealed by bifunctional cross-linking agents</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher scheme="https://scientific-publisher.data.istex.fr">ELSEVIER</publisher><availability><licence><p>elsevier</p></licence></availability><p scheme="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M"></p><date>1987</date></publicationStmt><notesStmt><note type="research-article" scheme="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</note><note type="journal" scheme="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</note><note>This research was supported by Public Health Service grants AI19545 and AI14710 from the National Institutes of Health, grant F1017 from the Robert A. Welch Foundation, and through generally appropriated funds from the State of Texas to the Cell Research Institute.</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a">Organization of the sindbis virus nucleocapsid as revealed by bifunctional cross-linking agents</title><author xml:id="author-0000"><persName><forename type="first">Kevin</forename><surname>Coombs</surname></persName><affiliation>The Cell Research Institute and Department of Microbiology The University of Texas at Austin, Austin, TX 78713, U.S.A.</affiliation></author><author xml:id="author-0001"><persName><forename type="first">Dennis T.</forename><surname>Brown</surname></persName><affiliation>The Cell Research Institute and Department of Microbiology The University of Texas at Austin, Austin, TX 78713, U.S.A.</affiliation></author><idno type="istex">1C03404FFB79D1D6E5A959D001D672FCA99662C5</idno><idno type="ark">ark:/67375/6H6-BRMPHTV3-T</idno><idno type="DOI">10.1016/0022-2836(87)90657-7</idno><idno type="PII">0022-2836(87)90657-7</idno></analytic><monogr><title level="j">Journal of Molecular Biology</title><title level="j" type="abbrev">YJMBI</title><idno type="pISSN">0022-2836</idno><idno type="PII">S0022-2836(00)X1131-X</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1987"></date><biblScope unit="volume">195</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="359">359</biblScope><biblScope unit="page" to="371">371</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1987</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Abstract: Purified Sindbis virus nucleocapsids were reacted with a variety of bifunctional proteinspecific cross-linking agents. The products were analyzed in concentration-gradient polyacrylamide gels and amounts of various products determined. These studies indicated that available lysine residues within adjacent capsid proteins in purified intact nucleocapsids are separated by 6 Å. The capsid proteins in intact nucleocapsids are crosslinked in a pattern predicted for discrete monomeric entities, rather than in dimeric or trimeric aggregates. Purified, soluble capsid protein exists in a conformation that differs from the arrangement of protein within nucleocapsids. These conformational differences suggest that topological changes may occur in the capsid protein during virus maturation. Cross-linked nucleocapsids that were treated with RNases resulted in the generation of RNA-free protein shells that retained hexagonal morphology, indicating that, together, the RNA and protein form the outer surface of the nucleocapsid. These data are used to produce a model of the Sindbis virus nucleocapsid in which the proteins are arranged quasiequivalently in a T = 4 icosahedral shell.</p></abstract></profileDesc><revisionDesc><change when="1986-12-17">Modified</change><change when="1987">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-BRMPHTV3-T/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>YJMBI</jid><aid>87906577</aid><ce:pii>0022-2836(87)90657-7</ce:pii><ce:doi>10.1016/0022-2836(87)90657-7</ce:doi><ce:copyright type="unknown" year="1987"></ce:copyright></item-info><head><ce:article-footnote><ce:label>☆</ce:label><ce:note-para>This research was supported by Public Health Service grants AI19545 and AI14710 from the National Institutes of Health, grant F1017 from the Robert A. Welch Foundation, and through generally appropriated funds from the State of Texas to the Cell Research Institute.</ce:note-para></ce:article-footnote><ce:title>Organization of the sindbis virus nucleocapsid as revealed by bifunctional cross-linking agents</ce:title><ce:author-group><ce:author><ce:given-name>Kevin</ce:given-name><ce:surname>Coombs</ce:surname></ce:author><ce:author><ce:given-name>Dennis T.</ce:given-name><ce:surname>Brown</ce:surname></ce:author><ce:affiliation><ce:textfn>The Cell Research Institute and Department of Microbiology The University of Texas at Austin, Austin, TX 78713, U.S.A.</ce:textfn></ce:affiliation></ce:author-group><ce:date-received day="29" month="9" year="1986"></ce:date-received><ce:date-revised day="17" month="12" year="1986"></ce:date-revised><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>Purified Sindbis virus nucleocapsids were reacted with a variety of bifunctional proteinspecific cross-linking agents. The products were analyzed in concentration-gradient polyacrylamide gels and amounts of various products determined. These studies indicated that available lysine residues within adjacent capsid proteins in purified intact nucleocapsids are separated by 6 Å. The capsid proteins in intact nucleocapsids are crosslinked in a pattern predicted for discrete monomeric entities, rather than in dimeric or trimeric aggregates. Purified, soluble capsid protein exists in a conformation that differs from the arrangement of protein within nucleocapsids. These conformational differences suggest that topological changes may occur in the capsid protein during virus maturation. Cross-linked nucleocapsids that were treated with RNases resulted in the generation of RNA-free protein shells that retained hexagonal morphology, indicating that, together, the RNA and protein form the outer surface of the nucleocapsid. These data are used to produce a model of the Sindbis virus nucleocapsid in which the proteins are arranged quasiequivalently in a <ce:italic>T</ce:italic> = 4 icosahedral shell.</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Organization of the sindbis virus nucleocapsid as revealed by bifunctional cross-linking agents</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Organization of the sindbis virus nucleocapsid as revealed by bifunctional cross-linking agents</title></titleInfo><name type="personal"><namePart type="given">Kevin</namePart><namePart type="family">Coombs</namePart><affiliation>The Cell Research Institute and Department of Microbiology The University of Texas at Austin, Austin, TX 78713, U.S.A.</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Dennis T.</namePart><namePart type="family">Brown</namePart><affiliation>The Cell Research Institute and Department of Microbiology The University of Texas at Austin, Austin, TX 78713, U.S.A.</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">1987</dateIssued><dateModified encoding="w3cdtf">1986-12-17</dateModified><copyrightDate encoding="w3cdtf">1987</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: Purified Sindbis virus nucleocapsids were reacted with a variety of bifunctional proteinspecific cross-linking agents. The products were analyzed in concentration-gradient polyacrylamide gels and amounts of various products determined. These studies indicated that available lysine residues within adjacent capsid proteins in purified intact nucleocapsids are separated by 6 Å. The capsid proteins in intact nucleocapsids are crosslinked in a pattern predicted for discrete monomeric entities, rather than in dimeric or trimeric aggregates. Purified, soluble capsid protein exists in a conformation that differs from the arrangement of protein within nucleocapsids. These conformational differences suggest that topological changes may occur in the capsid protein during virus maturation. Cross-linked nucleocapsids that were treated with RNases resulted in the generation of RNA-free protein shells that retained hexagonal morphology, indicating that, together, the RNA and protein form the outer surface of the nucleocapsid. These data are used to produce a model of the Sindbis virus nucleocapsid in which the proteins are arranged quasiequivalently in a T = 4 icosahedral shell.</abstract><note>This research was supported by Public Health Service grants AI19545 and AI14710 from the National Institutes of Health, grant F1017 from the Robert A. Welch Foundation, and through generally appropriated funds from the State of Texas to the Cell Research Institute.</note><relatedItem type="host"><titleInfo><title>Journal of Molecular Biology</title></titleInfo><titleInfo type="abbreviated"><title>YJMBI</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">1987</dateIssued></originInfo><identifier type="ISSN">0022-2836</identifier><identifier type="PII">S0022-2836(00)X1131-X</identifier><part><date>1987</date><detail type="volume"><number>195</number><caption>vol.</caption></detail><detail type="issue"><number>2</number><caption>no.</caption></detail><extent unit="issue-pages"><start>233</start><end>455</end></extent><extent unit="pages"><start>359</start><end>371</end></extent></part></relatedItem><identifier type="istex">1C03404FFB79D1D6E5A959D001D672FCA99662C5</identifier><identifier type="ark">ark:/67375/6H6-BRMPHTV3-T</identifier><identifier type="DOI">10.1016/0022-2836(87)90657-7</identifier><identifier type="PII">0022-2836(87)90657-7</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-BRMPHTV3-T/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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