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Activities of the feline immunodeficiency virus integrase protein produced in Escherichia coli
Retroviral DNA integration requires the activity of at least one viral protein, the integrase (IN) protein. We cloned and expressed the integrase gene of feline immunodeficiency virus (FIV) in Escherichia coli as a fusion to the male gene and purified the IN fusion protein by affinity chromatography...
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| Published in: | Journal of Virology 1994-03, Vol.68 (3), p.1468-1474 |
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| Main Authors: | , , |
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| Language: | English |
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| container_end_page | 1474 |
| container_issue | 3 |
| container_start_page | 1468 |
| container_title | Journal of Virology |
| container_volume | 68 |
| creator | Vink, C Linden, K.H. van der Plasterk, R.H.A |
| description | Retroviral DNA integration requires the activity of at least one viral protein, the integrase (IN) protein. We cloned and expressed the integrase gene of feline immunodeficiency virus (FIV) in Escherichia coli as a fusion to the male gene and purified the IN fusion protein by affinity chromatography. The protein is active in site-specific cleavage of the viral DNA ends, DNA strand transfer, and disintegration. FIV IN has a relaxed viral DNA substrate requirement: it cleaves and integrates FIV DNA termini, human immunodeficiency virus DNA ends, and Moloney murine leukemia virus DNA ends with high efficiencies. In the cleavage reaction, IN exposes a specific phosphodiester bond near the viral DNA end to nucleophilic attack. In vitro, either H2O, glycerol, or the 3' OH group of the viral DNA terminus can serve as nucleophile in this reaction. We found that FIV IN preferentially uses the 3' OH ends of the viral DNA as nucleophile, whereas HIV IN protein preferentially uses H2O and glycerol as nucleophiles |
| doi_str_mv | 10.1128/jvi.68.3.1468-1474.1994 |
| format | article |
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We cloned and expressed the integrase gene of feline immunodeficiency virus (FIV) in Escherichia coli as a fusion to the male gene and purified the IN fusion protein by affinity chromatography. The protein is active in site-specific cleavage of the viral DNA ends, DNA strand transfer, and disintegration. FIV IN has a relaxed viral DNA substrate requirement: it cleaves and integrates FIV DNA termini, human immunodeficiency virus DNA ends, and Moloney murine leukemia virus DNA ends with high efficiencies. In the cleavage reaction, IN exposes a specific phosphodiester bond near the viral DNA end to nucleophilic attack. In vitro, either H2O, glycerol, or the 3' OH group of the viral DNA terminus can serve as nucleophile in this reaction. We found that FIV IN preferentially uses the 3' OH ends of the viral DNA as nucleophile, whereas HIV IN protein preferentially uses H2O and glycerol as nucleophiles</description><identifier>ISSN: 0022-538X</identifier><identifier>EISSN: 1098-5514</identifier><identifier>DOI: 10.1128/jvi.68.3.1468-1474.1994</identifier><identifier>PMID: 8107210</identifier><language>eng</language><publisher>Washington, DC: American Society for Microbiology</publisher><subject>ADN ; ADN RECOMBINADO ; ADN RECOMBINE ; AIDS/HIV ; Amino Acid Sequence ; Base Sequence ; Biological and medical sciences ; Cloning, Molecular ; DNA Nucleotidyltransferases - genetics ; DNA Nucleotidyltransferases - isolation & purification ; DNA Nucleotidyltransferases - metabolism ; DNA Transposable Elements ; DNA-Binding Proteins - metabolism ; ESCHERICHIA COLI ; Escherichia coli - genetics ; feline immunodeficiency virus ; Fundamental and applied biological sciences. Psychology ; GENE ; GENES ; Immunodeficiency Virus, Feline - enzymology ; Integrases ; LENTIVIRINAE ; Microbiology ; Molecular Sequence Data ; PROTEINAS ; PROTEINE ; Recombinant Fusion Proteins - isolation & purification ; Recombinant Fusion Proteins - metabolism ; Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains ; Sequence Homology, Amino Acid ; Substrate Specificity ; TRANSFERENCIA DE GENES ; TRANSFERT DE GENE ; Virology ; VIRUS DE LOS ANIMALES ; VIRUS DES ANIMAUX ; Virus Integration - physiology</subject><ispartof>Journal of Virology, 1994-03, Vol.68 (3), p.1468-1474</ispartof><rights>1994 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c570t-59da42aae182f8f6cbf9773070644c62843f7f13ef49e0e0963317c88782c4293</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC236602/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC236602/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,3188,3189,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=3995856$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8107210$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Vink, C</creatorcontrib><creatorcontrib>Linden, K.H. van der</creatorcontrib><creatorcontrib>Plasterk, R.H.A</creatorcontrib><title>Activities of the feline immunodeficiency virus integrase protein produced in Escherichia coli</title><title>Journal of Virology</title><addtitle>J Virol</addtitle><description>Retroviral DNA integration requires the activity of at least one viral protein, the integrase (IN) protein. We cloned and expressed the integrase gene of feline immunodeficiency virus (FIV) in Escherichia coli as a fusion to the male gene and purified the IN fusion protein by affinity chromatography. The protein is active in site-specific cleavage of the viral DNA ends, DNA strand transfer, and disintegration. FIV IN has a relaxed viral DNA substrate requirement: it cleaves and integrates FIV DNA termini, human immunodeficiency virus DNA ends, and Moloney murine leukemia virus DNA ends with high efficiencies. In the cleavage reaction, IN exposes a specific phosphodiester bond near the viral DNA end to nucleophilic attack. In vitro, either H2O, glycerol, or the 3' OH group of the viral DNA terminus can serve as nucleophile in this reaction. We found that FIV IN preferentially uses the 3' OH ends of the viral DNA as nucleophile, whereas HIV IN protein preferentially uses H2O and glycerol as nucleophiles</description><subject>ADN</subject><subject>ADN RECOMBINADO</subject><subject>ADN RECOMBINE</subject><subject>AIDS/HIV</subject><subject>Amino Acid Sequence</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Cloning, Molecular</subject><subject>DNA Nucleotidyltransferases - genetics</subject><subject>DNA Nucleotidyltransferases - isolation & purification</subject><subject>DNA Nucleotidyltransferases - metabolism</subject><subject>DNA Transposable Elements</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>ESCHERICHIA COLI</subject><subject>Escherichia coli - genetics</subject><subject>feline immunodeficiency virus</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>GENE</subject><subject>GENES</subject><subject>Immunodeficiency Virus, Feline - enzymology</subject><subject>Integrases</subject><subject>LENTIVIRINAE</subject><subject>Microbiology</subject><subject>Molecular Sequence Data</subject><subject>PROTEINAS</subject><subject>PROTEINE</subject><subject>Recombinant Fusion Proteins - isolation & purification</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains</subject><subject>Sequence Homology, Amino Acid</subject><subject>Substrate Specificity</subject><subject>TRANSFERENCIA DE GENES</subject><subject>TRANSFERT DE GENE</subject><subject>Virology</subject><subject>VIRUS DE LOS ANIMALES</subject><subject>VIRUS DES ANIMAUX</subject><subject>Virus Integration - physiology</subject><issn>0022-538X</issn><issn>1098-5514</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><recordid>eNqFkUuL1EAURoMoYzv6BwQxgrhLrFfqsZjFMIwPGHChA64saiq3OndIUm1V0jL_3oRuGmfl6i6-892qyymKt5TUlDL98X6PtdQ1r6mQuqJCiZoaI54UG0qMrpqGiqfFhhDGqobrn8-LFznfE0KFkOKsONOUKEbJpvh16Sfc44SQyxjKqYMyQI8jlDgM8xhbCOgRRv9Q7jHNucRxgm1yGcpdihPguM529tAuUXmdfQcJfYeu9LHHl8Wz4PoMr47zvLj9dP3j6kt18-3z16vLm8o3ikxVY1onmHNANQs6SH8XjFKcKCKF8JJpwYMKlEMQBggQIzmnymutNPOCGX5eXBz27ua7AVoP45Rcb3cJB5cebHRoHycjdnYb95ZxKQlb-h-O_RR_z5AnO2D20PduhDhnqySXlAjxX5BKpRTlfAHVAfQp5pwgnD5DiV0V2kWhldpyuyq0q0K7Klyab_695dQ7Olvy98fcZe_6kNzoMZ8wbkyjG7lg7w5Yh9vuDyawLg-PH12Y1wcmuGjdNi1rbr-bhhgmJf8LsnK6gw</recordid><startdate>19940301</startdate><enddate>19940301</enddate><creator>Vink, C</creator><creator>Linden, K.H. van der</creator><creator>Plasterk, R.H.A</creator><general>American Society for Microbiology</general><scope>FBQ</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TM</scope><scope>7U9</scope><scope>H94</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19940301</creationdate><title>Activities of the feline immunodeficiency virus integrase protein produced in Escherichia coli</title><author>Vink, C ; Linden, K.H. van der ; Plasterk, R.H.A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c570t-59da42aae182f8f6cbf9773070644c62843f7f13ef49e0e0963317c88782c4293</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>ADN</topic><topic>ADN RECOMBINADO</topic><topic>ADN RECOMBINE</topic><topic>AIDS/HIV</topic><topic>Amino Acid Sequence</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Cloning, Molecular</topic><topic>DNA Nucleotidyltransferases - genetics</topic><topic>DNA Nucleotidyltransferases - isolation & purification</topic><topic>DNA Nucleotidyltransferases - metabolism</topic><topic>DNA Transposable Elements</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>ESCHERICHIA COLI</topic><topic>Escherichia coli - genetics</topic><topic>feline immunodeficiency virus</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>GENE</topic><topic>GENES</topic><topic>Immunodeficiency Virus, Feline - enzymology</topic><topic>Integrases</topic><topic>LENTIVIRINAE</topic><topic>Microbiology</topic><topic>Molecular Sequence Data</topic><topic>PROTEINAS</topic><topic>PROTEINE</topic><topic>Recombinant Fusion Proteins - isolation & purification</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains</topic><topic>Sequence Homology, Amino Acid</topic><topic>Substrate Specificity</topic><topic>TRANSFERENCIA DE GENES</topic><topic>TRANSFERT DE GENE</topic><topic>Virology</topic><topic>VIRUS DE LOS ANIMALES</topic><topic>VIRUS DES ANIMAUX</topic><topic>Virus Integration - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Vink, C</creatorcontrib><creatorcontrib>Linden, K.H. van der</creatorcontrib><creatorcontrib>Plasterk, R.H.A</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Journal of Virology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Vink, C</au><au>Linden, K.H. van der</au><au>Plasterk, R.H.A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Activities of the feline immunodeficiency virus integrase protein produced in Escherichia coli</atitle><jtitle>Journal of Virology</jtitle><addtitle>J Virol</addtitle><date>1994-03-01</date><risdate>1994</risdate><volume>68</volume><issue>3</issue><spage>1468</spage><epage>1474</epage><pages>1468-1474</pages><issn>0022-538X</issn><eissn>1098-5514</eissn><abstract>Retroviral DNA integration requires the activity of at least one viral protein, the integrase (IN) protein. We cloned and expressed the integrase gene of feline immunodeficiency virus (FIV) in Escherichia coli as a fusion to the male gene and purified the IN fusion protein by affinity chromatography. The protein is active in site-specific cleavage of the viral DNA ends, DNA strand transfer, and disintegration. FIV IN has a relaxed viral DNA substrate requirement: it cleaves and integrates FIV DNA termini, human immunodeficiency virus DNA ends, and Moloney murine leukemia virus DNA ends with high efficiencies. In the cleavage reaction, IN exposes a specific phosphodiester bond near the viral DNA end to nucleophilic attack. In vitro, either H2O, glycerol, or the 3' OH group of the viral DNA terminus can serve as nucleophile in this reaction. We found that FIV IN preferentially uses the 3' OH ends of the viral DNA as nucleophile, whereas HIV IN protein preferentially uses H2O and glycerol as nucleophiles</abstract><cop>Washington, DC</cop><pub>American Society for Microbiology</pub><pmid>8107210</pmid><doi>10.1128/jvi.68.3.1468-1474.1994</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0022-538X |
| ispartof | Journal of Virology, 1994-03, Vol.68 (3), p.1468-1474 |
| issn | 0022-538X 1098-5514 |
| language | eng |
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| source | American Society for Microbiology; PubMed (Medline) |
| subjects | ADN ADN RECOMBINADO ADN RECOMBINE AIDS/HIV Amino Acid Sequence Base Sequence Biological and medical sciences Cloning, Molecular DNA Nucleotidyltransferases - genetics DNA Nucleotidyltransferases - isolation & purification DNA Nucleotidyltransferases - metabolism DNA Transposable Elements DNA-Binding Proteins - metabolism ESCHERICHIA COLI Escherichia coli - genetics feline immunodeficiency virus Fundamental and applied biological sciences. Psychology GENE GENES Immunodeficiency Virus, Feline - enzymology Integrases LENTIVIRINAE Microbiology Molecular Sequence Data PROTEINAS PROTEINE Recombinant Fusion Proteins - isolation & purification Recombinant Fusion Proteins - metabolism Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains Sequence Homology, Amino Acid Substrate Specificity TRANSFERENCIA DE GENES TRANSFERT DE GENE Virology VIRUS DE LOS ANIMALES VIRUS DES ANIMAUX Virus Integration - physiology |
| title | Activities of the feline immunodeficiency virus integrase protein produced in Escherichia coli |
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