Moloney murine leukemia virus in protein from disrupted virions binds and specifically cleaves its target sequence in vitro
Identifieur interne : 000820 ( Istex/Corpus ); précédent : 000819; suivant : 000821Moloney murine leukemia virus in protein from disrupted virions binds and specifically cleaves its target sequence in vitro
Auteurs : Lance K. Ishimoto ; Mike Halperin ; Champouxi James J.Source :
- Virology [ 0042-6822 ] ; 1991.
English descriptors
- Teeft :
- Academic press, Assay, Avian myeloblastosis virus, Bind oligonucleotides, Binding activity, Binding assay, Binding reaction, Binding reactions, Champoux, Cleavage, Cleavage activity, Cleavage events, Cleavage product, Control oligonucleotide, Correct integration, Craigie, Dldc, Duplex, Duplex form, Duplex oligonucleotides, Endonuclease, Endonuclease activity, Extensive analysis, Fujiwara, Fusion product, Goff, Integration machinery, Integration reaction, Inverted, Major endonuclease activity, Moloney, Moloney murine leukemia virus, Murine, Nucleotide sequence, Oligonucleotide, Oligonucleotide substrates, Oligonucleotides, Path3 vector, Poly dldc, Polynucleotide kinase, Preimmune serum, Present evidence, Previous studies, Processing reaction, Processing step, Retarded mobility, Retroviral, Retroviral integration, Shift patterns, Sizing ladder, Specific binding, Specific cleavage, Such cleavage, Terminal sequences, Terminus, Unbound oligonucleotide, Unlabeled, Unlabeled lane, Varmus, Viral, Virion.
Abstract
Abstract: The integration of retroviral DNA plays an essential role in the viral life cycle. Previous studies of the Moloney murine leukemia virus (M-MuLV) have shown that viral integration is mediated by the integrase (IN) protein acting on the 13-bp inverted repeats that flank the linear viral DNA produced during reverse transcription. Prior studies have also shown that when the M-MuLV IN protein is produced in Escherichia coli it retains an ability to specifically associate with the viral inverted repeats (Krogstad and Champoux, 1990). In this study we present evidence that the IN protein present in detergent-disrupted virions is capable of specifically interacting with double-stranded oligonucleotides that correspond to the viral inverted repeats, and that this interaction may change after integration-related processing of the viral att sites. We further present evidence that, in vitro, detergent-disrupted virions are capable of specifically cleaving ds-IR oligonucleotides in an IN-dependent reaction that mimics the trimming step that precedes integration.
Url:
DOI: 10.1016/0042-6822(91)90066-K
Links to Exploration step
ISTEX:2B534489B47425183383795B62BDF92966B4B9F7Le document en format XML
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Ishimoto</name><affiliation><mods:affiliation>University of Washington, School of Medicine, Department of Microbiology SC-42, Seattle, Washington 98195, USA</mods:affiliation></affiliation></author><author><name sortKey="Halperin, Mike" sort="Halperin, Mike" uniqKey="Halperin M" first="Mike" last="Halperin">Mike Halperin</name><affiliation><mods:affiliation>University of Washington, School of Medicine, Department of Microbiology SC-42, Seattle, Washington 98195, USA</mods:affiliation></affiliation></author><author><name sortKey="James J, Champouxi" sort="James J, Champouxi" uniqKey="James J C" first="Champouxi" last="James J.">Champouxi James J.</name><affiliation><mods:affiliation>University of Washington, School of Medicine, Department of Microbiology SC-42, Seattle, Washington 98195, USA</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:2B534489B47425183383795B62BDF92966B4B9F7</idno><date when="1991" year="1991">1991</date><idno type="doi">10.1016/0042-6822(91)90066-K</idno><idno type="url">https://api.istex.fr/ark:/67375/6H6-Q4T6GC8V-L/fulltext.pdf</idno><idno type="wicri:Area/Istex/Corpus">000820</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">000820</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a">Moloney murine leukemia virus in protein from disrupted virions binds and specifically cleaves its target sequence in vitro</title><author><name sortKey="Ishimoto, Lance K" sort="Ishimoto, Lance K" uniqKey="Ishimoto L" first="Lance K." last="Ishimoto">Lance K. 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Previous studies of the Moloney murine leukemia virus (M-MuLV) have shown that viral integration is mediated by the integrase (IN) protein acting on the 13-bp inverted repeats that flank the linear viral DNA produced during reverse transcription. Prior studies have also shown that when the M-MuLV IN protein is produced in Escherichia coli it retains an ability to specifically associate with the viral inverted repeats (Krogstad and Champoux, 1990). In this study we present evidence that the IN protein present in detergent-disrupted virions is capable of specifically interacting with double-stranded oligonucleotides that correspond to the viral inverted repeats, and that this interaction may change after integration-related processing of the viral att sites. We further present evidence that, in vitro, detergent-disrupted virions are capable of specifically cleaving ds-IR oligonucleotides in an IN-dependent reaction that mimics the trimming step that precedes integration.</div></front></TEI><istex><corpusName>elsevier</corpusName><keywords><teeft><json:string>oligonucleotides</json:string><json:string>oligonucleotide</json:string><json:string>viral</json:string><json:string>virion</json:string><json:string>endonuclease</json:string><json:string>retroviral</json:string><json:string>dldc</json:string><json:string>champoux</json:string><json:string>unlabeled</json:string><json:string>moloney</json:string><json:string>varmus</json:string><json:string>murine</json:string><json:string>fujiwara</json:string><json:string>moloney murine leukemia virus</json:string><json:string>cleavage</json:string><json:string>control oligonucleotide</json:string><json:string>goff</json:string><json:string>craigie</json:string><json:string>unlabeled lane</json:string><json:string>binding activity</json:string><json:string>preimmune serum</json:string><json:string>assay</json:string><json:string>terminus</json:string><json:string>retroviral integration</json:string><json:string>academic press</json:string><json:string>previous studies</json:string><json:string>duplex</json:string><json:string>endonuclease activity</json:string><json:string>polynucleotide kinase</json:string><json:string>processing reaction</json:string><json:string>integration machinery</json:string><json:string>binding reactions</json:string><json:string>cleavage product</json:string><json:string>duplex oligonucleotides</json:string><json:string>poly dldc</json:string><json:string>inverted</json:string><json:string>duplex form</json:string><json:string>correct integration</json:string><json:string>integration reaction</json:string><json:string>sizing ladder</json:string><json:string>shift patterns</json:string><json:string>major endonuclease activity</json:string><json:string>nucleotide sequence</json:string><json:string>path3 vector</json:string><json:string>unbound oligonucleotide</json:string><json:string>binding reaction</json:string><json:string>processing step</json:string><json:string>present evidence</json:string><json:string>bind oligonucleotides</json:string><json:string>specific binding</json:string><json:string>binding assay</json:string><json:string>specific cleavage</json:string><json:string>oligonucleotide substrates</json:string><json:string>extensive analysis</json:string><json:string>terminal sequences</json:string><json:string>avian myeloblastosis virus</json:string><json:string>retarded mobility</json:string><json:string>cleavage events</json:string><json:string>cleavage activity</json:string><json:string>such cleavage</json:string><json:string>fusion product</json:string></teeft></keywords><author><json:item><name>Lance K. Ishimoto</name><affiliations><json:string>University of Washington, School of Medicine, Department of Microbiology SC-42, Seattle, Washington 98195, USA</json:string></affiliations></json:item><json:item><name>Mike Halperin</name><affiliations><json:string>University of Washington, School of Medicine, Department of Microbiology SC-42, Seattle, Washington 98195, USA</json:string></affiliations></json:item><json:item><name>Champouxi James J.</name><affiliations><json:string>University of Washington, School of Medicine, Department of Microbiology SC-42, Seattle, Washington 98195, USA</json:string></affiliations></json:item></author><arkIstex>ark:/67375/6H6-Q4T6GC8V-L</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>Abstract: The integration of retroviral DNA plays an essential role in the viral life cycle. Previous studies of the Moloney murine leukemia virus (M-MuLV) have shown that viral integration is mediated by the integrase (IN) protein acting on the 13-bp inverted repeats that flank the linear viral DNA produced during reverse transcription. Prior studies have also shown that when the M-MuLV IN protein is produced in Escherichia coli it retains an ability to specifically associate with the viral inverted repeats (Krogstad and Champoux, 1990). In this study we present evidence that the IN protein present in detergent-disrupted virions is capable of specifically interacting with double-stranded oligonucleotides that correspond to the viral inverted repeats, and that this interaction may change after integration-related processing of the viral att sites. We further present evidence that, in vitro, detergent-disrupted virions are capable of specifically cleaving ds-IR oligonucleotides in an IN-dependent reaction that mimics the trimming step that precedes integration.</abstract><qualityIndicators><score>8.86</score><pdfWordCount>5352</pdfWordCount><pdfCharCount>33840</pdfCharCount><pdfVersion>1.3</pdfVersion><pdfPageCount>8</pdfPageCount><pdfPageSize>612 x 792 pts (letter)</pdfPageSize><refBibsNative>true</refBibsNative><abstractWordCount>155</abstractWordCount><abstractCharCount>1076</abstractCharCount><keywordCount>0</keywordCount></qualityIndicators><title>Moloney murine leukemia virus in protein from disrupted virions binds and specifically cleaves its target sequence in vitro</title><pmid><json:string>1989383</json:string></pmid><pii><json:string>0042-6822(91)90066-K</json:string></pii><genre><json:string>research-article</json:string></genre><serie><title>Cell</title><language><json:string>unknown</json:string></language><volume>49</volume><pages><first>347</first><last>356</last></pages></serie><host><title>Virology</title><language><json:string>unknown</json:string></language><publicationDate>1991</publicationDate><issn><json:string>0042-6822</json:string></issn><pii><json:string>S0042-6822(00)X0257-7</json:string></pii><volume>180</volume><issue>2</issue><pages><first>527</first><last>534</last></pages><genre><json:string>journal</json:string></genre></host><namedEntities><unitex><date><json:string>1991</json:string></date><geogName></geogName><orgName><json:string>Sigma Chemical Co</json:string><json:string>Academic Press, Inc</json:string><json:string>American Cancer Society</json:string><json:string>Bethesda Research Laboratories</json:string><json:string>National Cancer Institute</json:string><json:string>Received September Department AND JAMES J</json:string><json:string>National Institute of Health Postdoctoral Fellowship</json:string><json:string>Public Health Service Grant CA51 605</json:string><json:string>Research Grant MV-232C</json:string></orgName><orgName_funder><json:string>Public Health Service Grant CA51 605</json:string><json:string>Research Grant MV-232C</json:string></orgName_funder><orgName_provider></orgName_provider><persName><json:string>J. J. Champoux</json:string><json:string>The</json:string><json:string>F. T. Ching</json:string><json:string>O.Ol</json:string><json:string>Stephanie Porter</json:string></persName><placeName><json:string>Krogstad</json:string></placeName><ref_url></ref_url><ref_bibl><json:string>Cobrinik et al., 1987</json:string><json:string>Donehower and Varmus, 1984</json:string><json:string>Katzman et al., 1989</json:string><json:string>Brown et al. (1989)</json:string><json:string>Panet and Baltimore (1987)</json:string><json:string>Roth et al., 1989</json:string><json:string>Colicelli and Goff, 1988</json:string><json:string>Roth et al., 1988</json:string><json:string>Fujiwara and Craigie, 1989</json:string><json:string>Fujiwara and Mizuuchi, 1988</json:string><json:string>Brown et al</json:string><json:string>Fujiwara and Mizuuchi (1988)</json:string><json:string>Fujrwara and Mizuuchi, 1988</json:string><json:string>Sen and Gilbert, 1990</json:string><json:string>Panet and Balti- INTRODUCTION Integration of retroviral DNA into the host chromosome is an essential step in the retroviral life cycle (Varmus and Swanstrom, 1985</json:string><json:string>Brown et al., 1989</json:string><json:string>Krogstad and Champoux, 1990</json:string><json:string>Fujiwara and Craigie (1989)</json:string></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/6H6-Q4T6GC8V-L</json:string></ark><categories><wos><json:string>1 - 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Previous studies of the Moloney murine leukemia virus (M-MuLV) have shown that viral integration is mediated by the integrase (IN) protein acting on the 13-bp inverted repeats that flank the linear viral DNA produced during reverse transcription. Prior studies have also shown that when the M-MuLV IN protein is produced in Escherichia coli it retains an ability to specifically associate with the viral inverted repeats (Krogstad and Champoux, 1990). In this study we present evidence that the IN protein present in detergent-disrupted virions is capable of specifically interacting with double-stranded oligonucleotides that correspond to the viral inverted repeats, and that this interaction may change after integration-related processing of the viral att sites. We further present evidence that, in vitro, detergent-disrupted virions are capable of specifically cleaving ds-IR oligonucleotides in an IN-dependent reaction that mimics the trimming step that precedes integration.</p></abstract></profileDesc><revisionDesc><change when="1991">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-Q4T6GC8V-L/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>YVIRO</jid><aid>9190066K</aid><ce:pii>0042-6822(91)90066-K</ce:pii><ce:doi>10.1016/0042-6822(91)90066-K</ce:doi><ce:copyright type="unknown" year="1991"></ce:copyright></item-info><head><ce:title>Moloney murine leukemia virus in protein from disrupted virions binds and specifically cleaves its target sequence <ce:italic>in vitro</ce:italic></ce:title><ce:author-group><ce:author><ce:given-name>Lance K.</ce:given-name><ce:surname>Ishimoto</ce:surname></ce:author><ce:author><ce:given-name>Mike</ce:given-name><ce:surname>Halperin</ce:surname></ce:author><ce:author><ce:surname>James J.</ce:surname><ce:given-name>Champouxi</ce:given-name><ce:cross-ref refid="COR1"><ce:sup>1</ce:sup></ce:cross-ref></ce:author><ce:affiliation><ce:textfn>University of Washington, School of Medicine, Department of Microbiology SC-42, Seattle, Washington 98195, USA</ce:textfn></ce:affiliation><ce:correspondence id="COR1"><ce:label>1</ce:label><ce:text>To whom reprint requests should be addressed.</ce:text></ce:correspondence></ce:author-group><ce:date-received day="13" month="9" year="1989"></ce:date-received><ce:date-accepted day="10" month="10" year="1990"></ce:date-accepted><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>The integration of retroviral DNA plays an essential role in the viral life cycle. Previous studies of the Moloney murine leukemia virus (M-MuLV) have shown that viral integration is mediated by the integrase (IN) protein acting on the 13-bp inverted repeats that flank the linear viral DNA produced during reverse transcription. Prior studies have also shown that when the M-MuLV IN protein is produced in <ce:italic>Escherichia coli</ce:italic> it retains an ability to specifically associate with the viral inverted repeats <ce:cross-ref refid="BIB19">(Krogstad and Champoux, 1990)</ce:cross-ref>. In this study we present evidence that the IN protein present in detergent-disrupted virions is capable of specifically interacting with double-stranded oligonucleotides that correspond to the viral inverted repeats, and that this interaction may change after integration-related processing of the viral <ce:italic>att</ce:italic> sites. We further present evidence that, <ce:italic>in vitro</ce:italic>, detergent-disrupted virions are capable of specifically cleaving ds-IR oligonucleotides in an IN-dependent reaction that mimics the trimming step that precedes integration.</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Moloney murine leukemia virus in protein from disrupted virions binds and specifically cleaves its target sequence in vitro</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Moloney murine leukemia virus in protein from disrupted virions binds and specifically cleaves its target sequence</title></titleInfo><name type="personal"><namePart type="given">Lance K.</namePart><namePart type="family">Ishimoto</namePart><affiliation>University of Washington, School of Medicine, Department of Microbiology SC-42, Seattle, Washington 98195, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Mike</namePart><namePart type="family">Halperin</namePart><affiliation>University of Washington, School of Medicine, Department of Microbiology SC-42, Seattle, Washington 98195, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Champouxi</namePart><namePart type="family">James J.</namePart><affiliation>University of Washington, School of Medicine, Department of Microbiology SC-42, Seattle, Washington 98195, USA</affiliation><description>To whom reprint requests should be addressed.</description><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">1991</dateIssued><copyrightDate encoding="w3cdtf">1991</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: The integration of retroviral DNA plays an essential role in the viral life cycle. Previous studies of the Moloney murine leukemia virus (M-MuLV) have shown that viral integration is mediated by the integrase (IN) protein acting on the 13-bp inverted repeats that flank the linear viral DNA produced during reverse transcription. Prior studies have also shown that when the M-MuLV IN protein is produced in Escherichia coli it retains an ability to specifically associate with the viral inverted repeats (Krogstad and Champoux, 1990). In this study we present evidence that the IN protein present in detergent-disrupted virions is capable of specifically interacting with double-stranded oligonucleotides that correspond to the viral inverted repeats, and that this interaction may change after integration-related processing of the viral att sites. We further present evidence that, in vitro, detergent-disrupted virions are capable of specifically cleaving ds-IR oligonucleotides in an IN-dependent reaction that mimics the trimming step that precedes integration.</abstract><relatedItem type="host"><titleInfo><title>Virology</title></titleInfo><titleInfo type="abbreviated"><title>YVIRO</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">1991</dateIssued></originInfo><identifier type="ISSN">0042-6822</identifier><identifier type="PII">S0042-6822(00)X0257-7</identifier><part><date>1991</date><detail type="volume"><number>180</number><caption>vol.</caption></detail><detail type="issue"><number>2</number><caption>no.</caption></detail><extent unit="issue-pages"><start>467</start><end>874</end></extent><extent unit="pages"><start>527</start><end>534</end></extent></part></relatedItem><identifier type="istex">2B534489B47425183383795B62BDF92966B4B9F7</identifier><identifier type="ark">ark:/67375/6H6-Q4T6GC8V-L</identifier><identifier type="DOI">10.1016/0042-6822(91)90066-K</identifier><identifier type="PII">0042-6822(91)90066-K</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-Q4T6GC8V-L/record.json</uri></json:item></metadata></istex></record>Pour manipuler ce document sous Unix (Dilib)
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