Terminal Association of Rad54 Protein with the Rad51-dsDNA Filament
Rad54 protein is a Snf2-related dsDNA-specific ATPase essential for homologous recombination mediated by Rad51 protein, the eukaryotic RecA ortholog. Snf2-related enzymes couple ATP hydrolysis with translocation on dsDNA to remodel or dissociate a wide variety of protein-dsDNA complexes. Rad54 and R...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2006-06, Vol.103 (26), p.9767-9772 |
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| container_issue | 26 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Kiianitsa, Konstantin Solinger, Jachen A. Heyer, Wolf-Dietrich |
| description | Rad54 protein is a Snf2-related dsDNA-specific ATPase essential for homologous recombination mediated by Rad51 protein, the eukaryotic RecA ortholog. Snf2-related enzymes couple ATP hydrolysis with translocation on dsDNA to remodel or dissociate a wide variety of protein-dsDNA complexes. Rad54 and Rad51 interact through species-specific contacts and mutually stimulate their biochemical activities. Specifically, Rad51 bound to dsDNA, the product of homologous recombination after DNA-strand exchange, stimulates the Rad54 ATPase up to 6-fold, leading to the turnover of Rad51 in the product complex. Electron microscopy visualized the Rad51-Rad54 interaction on dsDNA, showing that an oligomeric form of Rad54 associates preferentially with termini of the Rad51-dsDNA filament. Our data support a mechanism of processive dsDNA-Rad51 filament dissociation by the translocating Rad54 protein. |
| doi_str_mv | 10.1073/pnas.0604240103 |
| format | Article |
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Snf2-related enzymes couple ATP hydrolysis with translocation on dsDNA to remodel or dissociate a wide variety of protein-dsDNA complexes. Rad54 and Rad51 interact through species-specific contacts and mutually stimulate their biochemical activities. Specifically, Rad51 bound to dsDNA, the product of homologous recombination after DNA-strand exchange, stimulates the Rad54 ATPase up to 6-fold, leading to the turnover of Rad51 in the product complex. Electron microscopy visualized the Rad51-Rad54 interaction on dsDNA, showing that an oligomeric form of Rad54 associates preferentially with termini of the Rad51-dsDNA filament. Our data support a mechanism of processive dsDNA-Rad51 filament dissociation by the translocating Rad54 protein.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.0604240103</identifier><identifier>PMID: 16785421</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Adenosine Triphosphatases ; Biological Sciences ; DNA ; DNA - chemistry ; DNA - metabolism ; DNA Helicases ; DNA Repair Enzymes ; DNA-Binding Proteins - chemistry ; Gels ; Hydrolysis ; Kinetics ; Microscopy, Electron ; Molecules ; Monomers ; Nucleoproteins ; Particle interactions ; Protein Interaction Mapping ; Protein Transport ; Rad51 Recombinase - chemistry ; Rad51 Recombinase - metabolism ; Saccharomyces cerevisiae Proteins - chemistry ; Saccharomyces cerevisiae Proteins - metabolism ; Transcription Factors - chemistry ; Yeasts</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2006-06, Vol.103 (26), p.9767-9772</ispartof><rights>Copyright 2006 National Academy of Sciences of the United States of America</rights><rights>2006 by The National Academy of Sciences of the USA 2006</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c501t-f3cb61394e5dea8bf16bc75af5515ccb3f533468485eef17cc2fdf25b13cabf53</citedby><cites>FETCH-LOGICAL-c501t-f3cb61394e5dea8bf16bc75af5515ccb3f533468485eef17cc2fdf25b13cabf53</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/103/26.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/30050990$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/30050990$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27901,27902,53766,53768,57992,58225</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16785421$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kiianitsa, Konstantin</creatorcontrib><creatorcontrib>Solinger, Jachen A.</creatorcontrib><creatorcontrib>Heyer, Wolf-Dietrich</creatorcontrib><title>Terminal Association of Rad54 Protein with the Rad51-dsDNA Filament</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Rad54 protein is a Snf2-related dsDNA-specific ATPase essential for homologous recombination mediated by Rad51 protein, the eukaryotic RecA ortholog. Snf2-related enzymes couple ATP hydrolysis with translocation on dsDNA to remodel or dissociate a wide variety of protein-dsDNA complexes. Rad54 and Rad51 interact through species-specific contacts and mutually stimulate their biochemical activities. Specifically, Rad51 bound to dsDNA, the product of homologous recombination after DNA-strand exchange, stimulates the Rad54 ATPase up to 6-fold, leading to the turnover of Rad51 in the product complex. Electron microscopy visualized the Rad51-Rad54 interaction on dsDNA, showing that an oligomeric form of Rad54 associates preferentially with termini of the Rad51-dsDNA filament. Our data support a mechanism of processive dsDNA-Rad51 filament dissociation by the translocating Rad54 protein.</description><subject>Adenosine Triphosphatases</subject><subject>Biological Sciences</subject><subject>DNA</subject><subject>DNA - chemistry</subject><subject>DNA - metabolism</subject><subject>DNA Helicases</subject><subject>DNA Repair Enzymes</subject><subject>DNA-Binding Proteins - chemistry</subject><subject>Gels</subject><subject>Hydrolysis</subject><subject>Kinetics</subject><subject>Microscopy, Electron</subject><subject>Molecules</subject><subject>Monomers</subject><subject>Nucleoproteins</subject><subject>Particle interactions</subject><subject>Protein Interaction Mapping</subject><subject>Protein Transport</subject><subject>Rad51 Recombinase - chemistry</subject><subject>Rad51 Recombinase - metabolism</subject><subject>Saccharomyces cerevisiae Proteins - chemistry</subject><subject>Saccharomyces cerevisiae Proteins - metabolism</subject><subject>Transcription Factors - chemistry</subject><subject>Yeasts</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1v1DAQxS0EokvhzAnICXFJO2PHH7kgrbYUkCpAqJwtx7FZV0m82F4o_z1ZdtWFC5xGmvebNzN6hDxFOEOQ7HwzmXwGAhraAAK7RxYILdaiaeE-WQBQWatZOyGPcr4BgJYreEhOUEjFG4oLsrp2aQyTGaplztEGU0Kcquirz6bnTfUpxeLCVP0IZV2VtfvdxrrPFx-W1WUYzOim8pg88GbI7smhnpIvl2-uV-_qq49v36-WV7XlgKX2zHYCWds43jujOo-is5IbzzlyazvmOWONUI3iznmU1lLfe8o7ZNZ0s3hKXu99N9tudL2dVycz6E0Ko0k_dTRB_61MYa2_xu8aOVBO1Wzw8mCQ4rety0WPIVs3DGZycZu1UFxxAfS_IEoqUeLupPM9aFPMOTl_dw2C3iWkdwnpY0LzxPM_nzjyh0hm4NUB2E0e7ZimQrdSSO23w1DcbZnRF_9GZ-LZnrjJJaY7hAFwaFtgvwCnkK5c</recordid><startdate>20060627</startdate><enddate>20060627</enddate><creator>Kiianitsa, Konstantin</creator><creator>Solinger, Jachen A.</creator><creator>Heyer, Wolf-Dietrich</creator><general>National Academy of Sciences</general><general>National Acad Sciences</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>7X8</scope><scope>5PM</scope></search><sort><creationdate>20060627</creationdate><title>Terminal Association of Rad54 Protein with the Rad51-dsDNA Filament</title><author>Kiianitsa, Konstantin ; Solinger, Jachen A. ; Heyer, Wolf-Dietrich</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c501t-f3cb61394e5dea8bf16bc75af5515ccb3f533468485eef17cc2fdf25b13cabf53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Adenosine Triphosphatases</topic><topic>Biological Sciences</topic><topic>DNA</topic><topic>DNA - chemistry</topic><topic>DNA - metabolism</topic><topic>DNA Helicases</topic><topic>DNA Repair Enzymes</topic><topic>DNA-Binding Proteins - chemistry</topic><topic>Gels</topic><topic>Hydrolysis</topic><topic>Kinetics</topic><topic>Microscopy, Electron</topic><topic>Molecules</topic><topic>Monomers</topic><topic>Nucleoproteins</topic><topic>Particle interactions</topic><topic>Protein Interaction Mapping</topic><topic>Protein Transport</topic><topic>Rad51 Recombinase - chemistry</topic><topic>Rad51 Recombinase - metabolism</topic><topic>Saccharomyces cerevisiae Proteins - chemistry</topic><topic>Saccharomyces cerevisiae Proteins - metabolism</topic><topic>Transcription Factors - chemistry</topic><topic>Yeasts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kiianitsa, Konstantin</creatorcontrib><creatorcontrib>Solinger, Jachen A.</creatorcontrib><creatorcontrib>Heyer, Wolf-Dietrich</creatorcontrib><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>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kiianitsa, Konstantin</au><au>Solinger, Jachen A.</au><au>Heyer, Wolf-Dietrich</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Terminal Association of Rad54 Protein with the Rad51-dsDNA Filament</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2006-06-27</date><risdate>2006</risdate><volume>103</volume><issue>26</issue><spage>9767</spage><epage>9772</epage><pages>9767-9772</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>Rad54 protein is a Snf2-related dsDNA-specific ATPase essential for homologous recombination mediated by Rad51 protein, the eukaryotic RecA ortholog. Snf2-related enzymes couple ATP hydrolysis with translocation on dsDNA to remodel or dissociate a wide variety of protein-dsDNA complexes. Rad54 and Rad51 interact through species-specific contacts and mutually stimulate their biochemical activities. Specifically, Rad51 bound to dsDNA, the product of homologous recombination after DNA-strand exchange, stimulates the Rad54 ATPase up to 6-fold, leading to the turnover of Rad51 in the product complex. Electron microscopy visualized the Rad51-Rad54 interaction on dsDNA, showing that an oligomeric form of Rad54 associates preferentially with termini of the Rad51-dsDNA filament. Our data support a mechanism of processive dsDNA-Rad51 filament dissociation by the translocating Rad54 protein.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>16785421</pmid><doi>10.1073/pnas.0604240103</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| source | Jstor Complete Legacy; MEDLINE; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Adenosine Triphosphatases Biological Sciences DNA DNA - chemistry DNA - metabolism DNA Helicases DNA Repair Enzymes DNA-Binding Proteins - chemistry Gels Hydrolysis Kinetics Microscopy, Electron Molecules Monomers Nucleoproteins Particle interactions Protein Interaction Mapping Protein Transport Rad51 Recombinase - chemistry Rad51 Recombinase - metabolism Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - metabolism Transcription Factors - chemistry Yeasts |
| title | Terminal Association of Rad54 Protein with the Rad51-dsDNA Filament |
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