Bacteriophage P2 and P4 Morphogenesis: Identification and Characterization of the Portal Protein
Identifieur interne : 000922 ( Istex/Corpus ); précédent : 000921; suivant : 000923Bacteriophage P2 and P4 Morphogenesis: Identification and Characterization of the Portal Protein
Auteurs : Svein Rishovd ; Ole J. Marvik ; Erik Jacobsen ; Bj Rn H. LindqvistSource :
- Virology [ 0042-6822 ] ; 1994.
Abstract
Abstract: The portal structure has been implicated in several aspects of the bacteriophage life cycle, including capsid assembly initiation and DNA packaging. Here we present evidence that P2 gene Q codes for the P2 and P4 portal protein. First, microsequencing shows that capsid protein h6 is derived from gpQ, most probably by proteolytic cleavage, Second, antibodies against gpQ bind to the portal structure in disrupted P2 phage virions, as observed by electron microscopy. Third, gpQ partially purified from an overexpressing plasmid assembles into portal-like structures. We also show by microsequencing that capsid protein h7 is encoded by the P2 scaffold gene, O, and is probably derived from gpO by proteolytic cleavage. Previous work has demonstrated processing of the major capsid protein. Thus, all essential capsid proteins of P2 and P4 are proteolytically cleaved during the morphogenetic process.
Url:
DOI: 10.1006/viro.1994.1238
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Box 1125 Blindern, N-0317 Oslo, Norway</mods:affiliation></affiliation></author><author><name sortKey="Jacobsen, Erik" sort="Jacobsen, Erik" uniqKey="Jacobsen E" first="Erik" last="Jacobsen">Erik Jacobsen</name><affiliation><mods:affiliation>Institute of Biology and The Biotechnology Centre of Oslo, University of Oslo, Norway, P.O. Box 1125 Blindern, N-0317 Oslo, Norway</mods:affiliation></affiliation></author><author><name sortKey="Lindqvist, Bj Rn H" sort="Lindqvist, Bj Rn H" uniqKey="Lindqvist B" first="Bj Rn H." last="Lindqvist">Bj Rn H. Lindqvist</name><affiliation><mods:affiliation>Institute of Biology and The Biotechnology Centre of Oslo, University of Oslo, Norway, P.O. 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Lindqvist</name><affiliation><mods:affiliation>Institute of Biology and The Biotechnology Centre of Oslo, University of Oslo, Norway, P.O. Box 1125 Blindern, N-0317 Oslo, Norway</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">200</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="744">744</biblScope><biblScope unit="page" to="751">751</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: The portal structure has been implicated in several aspects of the bacteriophage life cycle, including capsid assembly initiation and DNA packaging. Here we present evidence that P2 gene Q codes for the P2 and P4 portal protein. First, microsequencing shows that capsid protein h6 is derived from gpQ, most probably by proteolytic cleavage, Second, antibodies against gpQ bind to the portal structure in disrupted P2 phage virions, as observed by electron microscopy. Third, gpQ partially purified from an overexpressing plasmid assembles into portal-like structures. We also show by microsequencing that capsid protein h7 is encoded by the P2 scaffold gene, O, and is probably derived from gpO by proteolytic cleavage. Previous work has demonstrated processing of the major capsid protein. Thus, all essential capsid proteins of P2 and P4 are proteolytically cleaved during the morphogenetic process.</div></front></TEI><istex><corpusName>elsevier</corpusName><author><json:item><name>Svein Rishovd</name><affiliations><json:string>Institute of Biology and The Biotechnology Centre of Oslo, University of Oslo, Norway, P.O. 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We also show by microsequencing that capsid protein h7 is encoded by the P2 scaffold gene, O, and is probably derived from gpO by proteolytic cleavage. Previous work has demonstrated processing of the major capsid protein. 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Box 1125 Blindern, N-0317 Oslo, Norway</affiliation></author><author xml:id="author-0001"><persName><forename type="first">Ole J.</forename><surname>Marvik</surname></persName><affiliation>Institute of Biology and The Biotechnology Centre of Oslo, University of Oslo, Norway, P.O. Box 1125 Blindern, N-0317 Oslo, Norway</affiliation></author><author xml:id="author-0002"><persName><forename type="first">Erik</forename><surname>Jacobsen</surname></persName><affiliation>Institute of Biology and The Biotechnology Centre of Oslo, University of Oslo, Norway, P.O. Box 1125 Blindern, N-0317 Oslo, Norway</affiliation></author><author xml:id="author-0003"><persName><forename type="first">Bjørn H.</forename><surname>Lindqvist</surname></persName><affiliation>Institute of Biology and The Biotechnology Centre of Oslo, University of Oslo, Norway, P.O. Box 1125 Blindern, N-0317 Oslo, Norway</affiliation></author><idno type="istex">E1DF5B8F5DCAD485A0D8132A84D6B40A9F02F273</idno><idno type="ark">ark:/67375/6H6-MV31F8PX-P</idno><idno type="DOI">10.1006/viro.1994.1238</idno><idno type="PII">S0042-6822(84)71238-4</idno></analytic><monogr><title level="j">Virology</title><title level="j" type="abbrev">YVIRO</title><idno type="pISSN">0042-6822</idno><idno type="PII">S0042-6822(00)X0168-7</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1994"></date><biblScope unit="volume">200</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="744">744</biblScope><biblScope unit="page" to="751">751</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1994</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Abstract: The portal structure has been implicated in several aspects of the bacteriophage life cycle, including capsid assembly initiation and DNA packaging. Here we present evidence that P2 gene Q codes for the P2 and P4 portal protein. First, microsequencing shows that capsid protein h6 is derived from gpQ, most probably by proteolytic cleavage, Second, antibodies against gpQ bind to the portal structure in disrupted P2 phage virions, as observed by electron microscopy. Third, gpQ partially purified from an overexpressing plasmid assembles into portal-like structures. We also show by microsequencing that capsid protein h7 is encoded by the P2 scaffold gene, O, and is probably derived from gpO by proteolytic cleavage. Previous work has demonstrated processing of the major capsid protein. 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Box 1125 Blindern, N-0317 Oslo, Norway</ce:textfn></ce:affiliation></ce:author-group><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>The portal structure has been implicated in several aspects of the bacteriophage life cycle, including capsid assembly initiation and DNA packaging. Here we present evidence that P2 gene Q codes for the P2 and P4 portal protein. First, microsequencing shows that capsid protein h6 is derived from gpQ, most probably by proteolytic cleavage, Second, antibodies against gpQ bind to the portal structure in disrupted P2 phage virions, as observed by electron microscopy. Third, gpQ partially purified from an overexpressing plasmid assembles into portal-like structures. We also show by microsequencing that capsid protein h7 is encoded by the P2 scaffold gene, <ce:italic>O</ce:italic>, and is probably derived from gpO by proteolytic cleavage. Previous work has demonstrated processing of the major capsid protein. Thus, all essential capsid proteins of P2 and P4 are proteolytically cleaved during the morphogenetic process.</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Bacteriophage P2 and P4 Morphogenesis: Identification and Characterization of the Portal Protein</title></titleInfo><titleInfo type="alternative" lang="en" contentType="CDATA"><title>Bacteriophage P2 and P4 Morphogenesis: Identification and Characterization of the Portal Protein</title></titleInfo><name type="personal"><namePart type="given">Svein</namePart><namePart type="family">Rishovd</namePart><affiliation>Institute of Biology and The Biotechnology Centre of Oslo, University of Oslo, Norway, P.O. Box 1125 Blindern, N-0317 Oslo, Norway</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Ole J.</namePart><namePart type="family">Marvik</namePart><affiliation>Institute of Biology and The Biotechnology Centre of Oslo, University of Oslo, Norway, P.O. Box 1125 Blindern, N-0317 Oslo, Norway</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Erik</namePart><namePart type="family">Jacobsen</namePart><affiliation>Institute of Biology and The Biotechnology Centre of Oslo, University of Oslo, Norway, P.O. Box 1125 Blindern, N-0317 Oslo, Norway</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Bjørn H.</namePart><namePart type="family">Lindqvist</namePart><affiliation>Institute of Biology and The Biotechnology Centre of Oslo, University of Oslo, Norway, P.O. Box 1125 Blindern, N-0317 Oslo, Norway</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">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: The portal structure has been implicated in several aspects of the bacteriophage life cycle, including capsid assembly initiation and DNA packaging. Here we present evidence that P2 gene Q codes for the P2 and P4 portal protein. First, microsequencing shows that capsid protein h6 is derived from gpQ, most probably by proteolytic cleavage, Second, antibodies against gpQ bind to the portal structure in disrupted P2 phage virions, as observed by electron microscopy. Third, gpQ partially purified from an overexpressing plasmid assembles into portal-like structures. We also show by microsequencing that capsid protein h7 is encoded by the P2 scaffold gene, O, and is probably derived from gpO by proteolytic cleavage. Previous work has demonstrated processing of the major capsid protein. 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