Human Papillomavirus (HPV) Origin-Binding Protein Associates with Mitotic Spindles to Enable Viral DNA Partitioning
Human papillomaviruses (HPVs) establish long-term infections in patients. The mechanism for extrachromosomal HPV DNA persistence in cycling cells is unknown. We show that HPV origin-containing plasmids partition as minichromosomes, attributable to an association of the viral origin recognition prote...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2004-03, Vol.101 (12), p.4030-4035 |
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| creator | Van Tine, Brian A. Dao, Luan D. Wu, Shwu-Yuan Sonbuchner, Timothy M. Lin, Biing Yuan Zou, Nianxiang Chiang, Cheng-Ming Broker, Thomas R. Chow, Louise T. Lehman, I. Robert |
| description | Human papillomaviruses (HPVs) establish long-term infections in patients. The mechanism for extrachromosomal HPV DNA persistence in cycling cells is unknown. We show that HPV origin-containing plasmids partition as minichromosomes, attributable to an association of the viral origin recognition protein E2 with mitotic spindles. α-, β-, and γ-tubulins were pulled down with a tagged E2. The N-terminal transacting and C-terminal protein dimerization/DNA binding domains independently associated with the spindles. We suggest that this E2 property enables these viruses to establish persistence. Its implication for HPV oncogenesis is presented. |
| doi_str_mv | 10.1073/pnas.0306848101 |
| format | Article |
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Its implication for HPV oncogenesis is presented.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.0306848101</identifier><identifier>PMID: 15020762</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Biochemistry ; Biological Sciences ; Cell lines ; Centrosome - metabolism ; Centrosomes ; Chromosomes ; Daughter cells ; DNA ; DNA, Viral - metabolism ; DNA-Binding Proteins - metabolism ; Genes, Reporter ; Genetic Vectors ; HEK293 cells ; HeLa cells ; Human papillomavirus ; Human papillomavirus 11 ; Humans ; Microtubule-Organizing Center - metabolism ; Microtubules - metabolism ; Mitotic spindle apparatus ; Papillomaviridae - metabolism ; Plasmids ; Protein Structure, Tertiary ; Proteins ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - metabolism ; Spindle Apparatus - metabolism ; Viral Proteins - metabolism ; Viruses</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2004-03, Vol.101 (12), p.4030-4035</ispartof><rights>Copyright 1993/2004 The National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Mar 23, 2004</rights><rights>Copyright © 2004, The National Academy of Sciences 2004</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c524t-c1e8b8227f5675b34d89852ce87eba45ea277a36c9cf9f41f293f4ce070a18283</citedby><cites>FETCH-LOGICAL-c524t-c1e8b8227f5675b34d89852ce87eba45ea277a36c9cf9f41f293f4ce070a18283</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/101/12.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/3371557$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/3371557$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,724,777,781,800,882,27905,27906,53772,53774,57998,58231</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15020762$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Van Tine, Brian A.</creatorcontrib><creatorcontrib>Dao, Luan D.</creatorcontrib><creatorcontrib>Wu, Shwu-Yuan</creatorcontrib><creatorcontrib>Sonbuchner, Timothy M.</creatorcontrib><creatorcontrib>Lin, Biing Yuan</creatorcontrib><creatorcontrib>Zou, Nianxiang</creatorcontrib><creatorcontrib>Chiang, Cheng-Ming</creatorcontrib><creatorcontrib>Broker, Thomas R.</creatorcontrib><creatorcontrib>Chow, Louise T.</creatorcontrib><creatorcontrib>Lehman, I. Robert</creatorcontrib><title>Human Papillomavirus (HPV) Origin-Binding Protein Associates with Mitotic Spindles to Enable Viral DNA Partitioning</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Human papillomaviruses (HPVs) establish long-term infections in patients. The mechanism for extrachromosomal HPV DNA persistence in cycling cells is unknown. We show that HPV origin-containing plasmids partition as minichromosomes, attributable to an association of the viral origin recognition protein E2 with mitotic spindles. α-, β-, and γ-tubulins were pulled down with a tagged E2. The N-terminal transacting and C-terminal protein dimerization/DNA binding domains independently associated with the spindles. We suggest that this E2 property enables these viruses to establish persistence. Its implication for HPV oncogenesis is presented.</description><subject>Biochemistry</subject><subject>Biological Sciences</subject><subject>Cell lines</subject><subject>Centrosome - metabolism</subject><subject>Centrosomes</subject><subject>Chromosomes</subject><subject>Daughter cells</subject><subject>DNA</subject><subject>DNA, Viral - metabolism</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Genes, Reporter</subject><subject>Genetic Vectors</subject><subject>HEK293 cells</subject><subject>HeLa cells</subject><subject>Human papillomavirus</subject><subject>Human papillomavirus 11</subject><subject>Humans</subject><subject>Microtubule-Organizing Center - metabolism</subject><subject>Microtubules - metabolism</subject><subject>Mitotic spindle apparatus</subject><subject>Papillomaviridae - metabolism</subject><subject>Plasmids</subject><subject>Protein Structure, Tertiary</subject><subject>Proteins</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Spindle Apparatus - metabolism</subject><subject>Viral Proteins - metabolism</subject><subject>Viruses</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc9v0zAYhiMEYmVw5oLA4jCNQ7bPPxI7Bw5lDIo0WCVgV8t1nc5VYme2s8F_j6tWK3CAkyX7eR9_9lsUzzGcYOD0dHAqngCFWjCBAT8oJhgaXNasgYfFBIDwUjDCDoonMa4BoKkEPC4OcAUEeE0mRZyNvXJorgbbdb5XtzaMER3P5ldv0GWwK-vKd9YtrVuhefDJWIemMXptVTIR3dl0jT7b5JPV6OuQwS7vJo_OnVp0Bl3ZoDr0_ss0XxCSTda7bHpaPGpVF82z3XpYfP9w_u1sVl5cfvx0Nr0odUVYKjU2YiEI4W1V82pB2VI0oiLaCG4WilVGEc4VrXWj26ZluCUNbZk2wEFhQQQ9LN5uvcO46M1SG5fyOHIItlfhp_TKyj9PnL2WK38rqWB1Azl_tMsHfzOamGRvozZdp5zxY5Qc86pmjP4XxLxhjNUb4-u_wLUfg8ufIAlgyjiDOkOnW0gHH2Mw7f3EGOSmdblpXe5bz4mXvz90z-9qzsDxDtgk9zosMZEsm2Q7dl0yP1JGX_0bzcSLLbGOyYd7hFKOq4rTXypiyoo</recordid><startdate>20040323</startdate><enddate>20040323</enddate><creator>Van Tine, Brian A.</creator><creator>Dao, Luan D.</creator><creator>Wu, Shwu-Yuan</creator><creator>Sonbuchner, Timothy M.</creator><creator>Lin, Biing Yuan</creator><creator>Zou, Nianxiang</creator><creator>Chiang, Cheng-Ming</creator><creator>Broker, Thomas R.</creator><creator>Chow, Louise T.</creator><creator>Lehman, I. 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Robert</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Human Papillomavirus (HPV) Origin-Binding Protein Associates with Mitotic Spindles to Enable Viral DNA Partitioning</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2004-03-23</date><risdate>2004</risdate><volume>101</volume><issue>12</issue><spage>4030</spage><epage>4035</epage><pages>4030-4035</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>Human papillomaviruses (HPVs) establish long-term infections in patients. The mechanism for extrachromosomal HPV DNA persistence in cycling cells is unknown. We show that HPV origin-containing plasmids partition as minichromosomes, attributable to an association of the viral origin recognition protein E2 with mitotic spindles. α-, β-, and γ-tubulins were pulled down with a tagged E2. The N-terminal transacting and C-terminal protein dimerization/DNA binding domains independently associated with the spindles. We suggest that this E2 property enables these viruses to establish persistence. Its implication for HPV oncogenesis is presented.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>15020762</pmid><doi>10.1073/pnas.0306848101</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Biochemistry Biological Sciences Cell lines Centrosome - metabolism Centrosomes Chromosomes Daughter cells DNA DNA, Viral - metabolism DNA-Binding Proteins - metabolism Genes, Reporter Genetic Vectors HEK293 cells HeLa cells Human papillomavirus Human papillomavirus 11 Humans Microtubule-Organizing Center - metabolism Microtubules - metabolism Mitotic spindle apparatus Papillomaviridae - metabolism Plasmids Protein Structure, Tertiary Proteins Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism Spindle Apparatus - metabolism Viral Proteins - metabolism Viruses |
| title | Human Papillomavirus (HPV) Origin-Binding Protein Associates with Mitotic Spindles to Enable Viral DNA Partitioning |
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