Solution structure of the cellular factor BAF responsible for protecting retroviral DNA from autointegration
The solution structure of the human barrier-to-autointegration factor, BAF, a 21,000 M r dimer, has been solved by NMR, including extensive use of dipolar couplings which provide a priori long range structural information. BAF is a highly evolutionarily conserved DNA binding protein that is responsi...
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| Veröffentlicht in: | Nature Structural Biology 1998-10, Vol.5 (10), p.903-909 |
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| container_title | Nature Structural Biology |
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| creator | Cai, Mengli Huang, Ying Zheng, Ronglan Wei, Shui-Qing Ghirlando, Rodolfo Lee, Myung Soo Craigie, Robert Gronenborn, Angela M. Clore, G. Marius |
| description | The solution structure of the human barrier-to-autointegration factor, BAF, a 21,000
M
r
dimer, has been solved by NMR, including extensive use of dipolar couplings which provide
a priori
long range structural information. BAF is a highly evolutionarily conserved DNA binding protein that is responsible for inhibiting autointegration of retroviral DNA, thereby promoting integration of retroviral DNA into the host chromosome. BAF is largely helical, and each subunit is composed of five helices. The dimer is elongated in shape and the dimer interface comprises principally hydrophobic contacts supplemented by a single salt bridge. Despite the absence of any sequence similarity to any other known protein family, the topology of helices 3–5 is similar to that of a number of DNA binding proteins, with helices 4 and 5 constituting a helix-turn-helix motif. A model for the interaction of BAF with DNA that is consistent with structural and mutagenesis data is proposed. |
| doi_str_mv | 10.1038/2345 |
| format | Article |
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M
r
dimer, has been solved by NMR, including extensive use of dipolar couplings which provide
a priori
long range structural information. BAF is a highly evolutionarily conserved DNA binding protein that is responsible for inhibiting autointegration of retroviral DNA, thereby promoting integration of retroviral DNA into the host chromosome. BAF is largely helical, and each subunit is composed of five helices. The dimer is elongated in shape and the dimer interface comprises principally hydrophobic contacts supplemented by a single salt bridge. Despite the absence of any sequence similarity to any other known protein family, the topology of helices 3–5 is similar to that of a number of DNA binding proteins, with helices 4 and 5 constituting a helix-turn-helix motif. A model for the interaction of BAF with DNA that is consistent with structural and mutagenesis data is proposed.</description><identifier>ISSN: 1072-8368</identifier><identifier>EISSN: 1545-9985</identifier><identifier>DOI: 10.1038/2345</identifier><identifier>PMID: 9783751</identifier><language>eng</language><publisher>New York: Nature Publishing Group US</publisher><subject>Amino Acid Sequence ; Biochemistry ; Biological Microscopy ; Biomedical and Life Sciences ; Crystallography, X-Ray ; Dimerization ; DNA - chemistry ; DNA, Viral - genetics ; DNA-Binding Proteins - chemistry ; Helix-Turn-Helix Motifs ; Humans ; Life Sciences ; Membrane Biology ; Models, Molecular ; Molecular Sequence Data ; Nuclear Magnetic Resonance, Biomolecular ; Nuclear Proteins ; Nucleic Acid Conformation ; Protein Structure ; Protein Structure, Secondary ; Retroviridae - physiology ; Retrovirus ; Sequence Homology, Amino Acid ; Virus Integration - physiology</subject><ispartof>Nature Structural Biology, 1998-10, Vol.5 (10), p.903-909</ispartof><rights>Nature America Inc. 1998</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c331t-b72db5b77654bf8f2487c42e59296334838c0a869daf444ae16f5895ba7c0f83</citedby><cites>FETCH-LOGICAL-c331t-b72db5b77654bf8f2487c42e59296334838c0a869daf444ae16f5895ba7c0f83</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/2345$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/2345$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27903,27904,41467,42536,51298</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9783751$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Cai, Mengli</creatorcontrib><creatorcontrib>Huang, Ying</creatorcontrib><creatorcontrib>Zheng, Ronglan</creatorcontrib><creatorcontrib>Wei, Shui-Qing</creatorcontrib><creatorcontrib>Ghirlando, Rodolfo</creatorcontrib><creatorcontrib>Lee, Myung Soo</creatorcontrib><creatorcontrib>Craigie, Robert</creatorcontrib><creatorcontrib>Gronenborn, Angela M.</creatorcontrib><creatorcontrib>Clore, G. Marius</creatorcontrib><title>Solution structure of the cellular factor BAF responsible for protecting retroviral DNA from autointegration</title><title>Nature Structural Biology</title><addtitle>Nat Struct Mol Biol</addtitle><addtitle>Nat Struct Biol</addtitle><description>The solution structure of the human barrier-to-autointegration factor, BAF, a 21,000
M
r
dimer, has been solved by NMR, including extensive use of dipolar couplings which provide
a priori
long range structural information. BAF is a highly evolutionarily conserved DNA binding protein that is responsible for inhibiting autointegration of retroviral DNA, thereby promoting integration of retroviral DNA into the host chromosome. BAF is largely helical, and each subunit is composed of five helices. The dimer is elongated in shape and the dimer interface comprises principally hydrophobic contacts supplemented by a single salt bridge. Despite the absence of any sequence similarity to any other known protein family, the topology of helices 3–5 is similar to that of a number of DNA binding proteins, with helices 4 and 5 constituting a helix-turn-helix motif. A model for the interaction of BAF with DNA that is consistent with structural and mutagenesis data is proposed.</description><subject>Amino Acid Sequence</subject><subject>Biochemistry</subject><subject>Biological Microscopy</subject><subject>Biomedical and Life Sciences</subject><subject>Crystallography, X-Ray</subject><subject>Dimerization</subject><subject>DNA - chemistry</subject><subject>DNA, Viral - genetics</subject><subject>DNA-Binding Proteins - chemistry</subject><subject>Helix-Turn-Helix Motifs</subject><subject>Humans</subject><subject>Life Sciences</subject><subject>Membrane Biology</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Nuclear Magnetic Resonance, Biomolecular</subject><subject>Nuclear Proteins</subject><subject>Nucleic Acid Conformation</subject><subject>Protein Structure</subject><subject>Protein Structure, Secondary</subject><subject>Retroviridae - physiology</subject><subject>Retrovirus</subject><subject>Sequence Homology, Amino Acid</subject><subject>Virus Integration - physiology</subject><issn>1072-8368</issn><issn>1545-9985</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkE9LAzEQxYMotbZ-BCEH9baabJJN9lirVaHowd6XbJrULemm5o_gtzdLi-Bphvk93sw8AKYY3WFExH1JKDsBY8woK-pasNPcI14WglTiHFyEsEWoZIyTERjVXBDO8BjYD2dT7FwPQ_RJxeQ1dAbGTw2VtjZZ6aGRKjoPH2YL6HXYuz50rdXQ5Nneu6hV7PpNRtG7785LCx_fZtB4t4MyRdf1UW-8HHZMwZmRNujLY52A1eJpNX8plu_Pr_PZslCE4Fi0vFy3rOW8YrQ1wpRUcEVLzeqyrgihggiFpKjqtTSUUqlxZZioWSu5QkaQCbg92ObrvpIOsdl1YfhG9tql0GCOMWECZeH1Qai8C8Fr0-x9t5P-p8GoGTJthkyz7Orol9qdXv-JjiFmfnPgIZN-o32zdcn3-cP_Pr8GT34G</recordid><startdate>19981001</startdate><enddate>19981001</enddate><creator>Cai, Mengli</creator><creator>Huang, Ying</creator><creator>Zheng, Ronglan</creator><creator>Wei, Shui-Qing</creator><creator>Ghirlando, Rodolfo</creator><creator>Lee, Myung Soo</creator><creator>Craigie, Robert</creator><creator>Gronenborn, Angela M.</creator><creator>Clore, G. Marius</creator><general>Nature Publishing Group US</general><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></search><sort><creationdate>19981001</creationdate><title>Solution structure of the cellular factor BAF responsible for protecting retroviral DNA from autointegration</title><author>Cai, Mengli ; Huang, Ying ; Zheng, Ronglan ; Wei, Shui-Qing ; Ghirlando, Rodolfo ; Lee, Myung Soo ; Craigie, Robert ; Gronenborn, Angela M. ; Clore, G. Marius</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c331t-b72db5b77654bf8f2487c42e59296334838c0a869daf444ae16f5895ba7c0f83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Amino Acid Sequence</topic><topic>Biochemistry</topic><topic>Biological Microscopy</topic><topic>Biomedical and Life Sciences</topic><topic>Crystallography, X-Ray</topic><topic>Dimerization</topic><topic>DNA - chemistry</topic><topic>DNA, Viral - genetics</topic><topic>DNA-Binding Proteins - chemistry</topic><topic>Helix-Turn-Helix Motifs</topic><topic>Humans</topic><topic>Life Sciences</topic><topic>Membrane Biology</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Nuclear Magnetic Resonance, Biomolecular</topic><topic>Nuclear Proteins</topic><topic>Nucleic Acid Conformation</topic><topic>Protein Structure</topic><topic>Protein Structure, Secondary</topic><topic>Retroviridae - physiology</topic><topic>Retrovirus</topic><topic>Sequence Homology, Amino Acid</topic><topic>Virus Integration - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cai, Mengli</creatorcontrib><creatorcontrib>Huang, Ying</creatorcontrib><creatorcontrib>Zheng, Ronglan</creatorcontrib><creatorcontrib>Wei, Shui-Qing</creatorcontrib><creatorcontrib>Ghirlando, Rodolfo</creatorcontrib><creatorcontrib>Lee, Myung Soo</creatorcontrib><creatorcontrib>Craigie, Robert</creatorcontrib><creatorcontrib>Gronenborn, Angela M.</creatorcontrib><creatorcontrib>Clore, G. 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Marius</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Solution structure of the cellular factor BAF responsible for protecting retroviral DNA from autointegration</atitle><jtitle>Nature Structural Biology</jtitle><stitle>Nat Struct Mol Biol</stitle><addtitle>Nat Struct Biol</addtitle><date>1998-10-01</date><risdate>1998</risdate><volume>5</volume><issue>10</issue><spage>903</spage><epage>909</epage><pages>903-909</pages><issn>1072-8368</issn><eissn>1545-9985</eissn><abstract>The solution structure of the human barrier-to-autointegration factor, BAF, a 21,000
M
r
dimer, has been solved by NMR, including extensive use of dipolar couplings which provide
a priori
long range structural information. BAF is a highly evolutionarily conserved DNA binding protein that is responsible for inhibiting autointegration of retroviral DNA, thereby promoting integration of retroviral DNA into the host chromosome. BAF is largely helical, and each subunit is composed of five helices. The dimer is elongated in shape and the dimer interface comprises principally hydrophobic contacts supplemented by a single salt bridge. Despite the absence of any sequence similarity to any other known protein family, the topology of helices 3–5 is similar to that of a number of DNA binding proteins, with helices 4 and 5 constituting a helix-turn-helix motif. A model for the interaction of BAF with DNA that is consistent with structural and mutagenesis data is proposed.</abstract><cop>New York</cop><pub>Nature Publishing Group US</pub><pmid>9783751</pmid><doi>10.1038/2345</doi><tpages>7</tpages></addata></record> |
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| subjects | Amino Acid Sequence Biochemistry Biological Microscopy Biomedical and Life Sciences Crystallography, X-Ray Dimerization DNA - chemistry DNA, Viral - genetics DNA-Binding Proteins - chemistry Helix-Turn-Helix Motifs Humans Life Sciences Membrane Biology Models, Molecular Molecular Sequence Data Nuclear Magnetic Resonance, Biomolecular Nuclear Proteins Nucleic Acid Conformation Protein Structure Protein Structure, Secondary Retroviridae - physiology Retrovirus Sequence Homology, Amino Acid Virus Integration - physiology |
| title | Solution structure of the cellular factor BAF responsible for protecting retroviral DNA from autointegration |
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