double-hexameric MCM2-7 complex is loaded onto origin DNA during licensing of eukaryotic DNA replication
During pre-replication complex (pre-RC) formation, origin recognition complex (ORC), Cdc6, and Cdt1 cooperatively load the 6-subunit mini chromosome maintenance (MCM2-7) complex onto DNA. Loading of MCM2-7 is a prerequisite for DNA licensing that restricts DNA replication to once per cell cycle. Dur...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2009-12, Vol.106 (48), p.20240-20245 |
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| creator | Evrin, Cecile Clarke, Pippa Zech, Juergen Lurz, Rudi Sun, Jingchuan Uhle, Stefan Li, Huilin Stillman, Bruce Speck, Christian |
| description | During pre-replication complex (pre-RC) formation, origin recognition complex (ORC), Cdc6, and Cdt1 cooperatively load the 6-subunit mini chromosome maintenance (MCM2-7) complex onto DNA. Loading of MCM2-7 is a prerequisite for DNA licensing that restricts DNA replication to once per cell cycle. During S phase MCM2-7 functions as part of the replicative helicase but within the pre-RC MCM2-7 is inactive. The organization of replicative DNA helicases before and after loading onto DNA has been studied in bacteria and viruses but not eukaryotes and is of major importance for understanding the MCM2-7 loading mechanism and replisome assembly. Lack of an efficient reconstituted pre-RC system has hindered the detailed mechanistic and structural analysis of MCM2-7 loading for a long time. We have reconstituted Saccharomyces cerevisiae pre-RC formation with purified proteins and showed efficient loading of MCM2-7 onto origin DNA in vitro. MCM2-7 loading was found to be dependent on the presence of all pre-RC proteins, origin DNA, and ATP hydrolysis. The quaternary structure of MCM2-7 changes during pre-RC formation: MCM2-7 before loading is a single hexamer in solution but is transformed into a double-hexamer during pre-RC formation. Using electron microscopy (EM), we observed that loaded MCM2-7 encircles DNA. The loaded MCM2-7 complex can slide on DNA, and sliding is not directional. Our results provide key insights into mechanisms of pre-RC formation and have important implications for understanding the role of the MCM2-7 in establishment of bidirectional replication forks. |
| doi_str_mv | 10.1073/pnas.0911500106 |
| format | Article |
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Loading of MCM2-7 is a prerequisite for DNA licensing that restricts DNA replication to once per cell cycle. During S phase MCM2-7 functions as part of the replicative helicase but within the pre-RC MCM2-7 is inactive. The organization of replicative DNA helicases before and after loading onto DNA has been studied in bacteria and viruses but not eukaryotes and is of major importance for understanding the MCM2-7 loading mechanism and replisome assembly. Lack of an efficient reconstituted pre-RC system has hindered the detailed mechanistic and structural analysis of MCM2-7 loading for a long time. We have reconstituted Saccharomyces cerevisiae pre-RC formation with purified proteins and showed efficient loading of MCM2-7 onto origin DNA in vitro. MCM2-7 loading was found to be dependent on the presence of all pre-RC proteins, origin DNA, and ATP hydrolysis. The quaternary structure of MCM2-7 changes during pre-RC formation: MCM2-7 before loading is a single hexamer in solution but is transformed into a double-hexamer during pre-RC formation. Using electron microscopy (EM), we observed that loaded MCM2-7 encircles DNA. The loaded MCM2-7 complex can slide on DNA, and sliding is not directional. Our results provide key insights into mechanisms of pre-RC formation and have important implications for understanding the role of the MCM2-7 in establishment of bidirectional replication forks.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.0911500106</identifier><identifier>PMID: 19910535</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>60 APPLIED LIFE SCIENCES ; Animals ; BACTERIA ; BASIC BIOLOGICAL SCIENCES ; Biological Sciences ; CELL CYCLE ; Chromatography, Gel ; Chromosomal Proteins, Non-Histone - metabolism ; CHROMOSOMES ; Cloning, Molecular ; Deoxyribonucleic acid ; DNA ; DNA HELICASES ; DNA Helicases - metabolism ; DNA REPLICATION ; DNA Replication - physiology ; DNA-Binding Proteins - metabolism ; ELECTRON MICROSCOPY ; Eukaryotes ; helicase ; HYDROLYSIS ; IN VITRO ; initiation ; LICENSING ; MAINTENANCE ; Microscopy, Electron ; mini chromosome maintenance ; Models, Molecular ; Molecular structure ; Multiprotein Complexes - metabolism ; Multiprotein Complexes - ultrastructure ; Oligonucleotides ; ORC ; ORIGIN ; Plasmids ; pre-RC ; Protein Conformation ; PROTEINS ; Replication origin ; SACCHAROMYCES CEREVISIAE ; Saccharomyces cerevisiae Proteins - metabolism ; Salts ; Viral tumor antigens ; VIRUSES ; Xenopus ; Yeast ; Yeasts</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2009-12, Vol.106 (48), p.20240-20245</ispartof><rights>Copyright National Academy of Sciences Dec 1, 2009</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c617t-89999fd20b3a25c3bf84a8a0a81d416aca1ceb9d7ee979cf45855399bdbecf433</citedby><cites>FETCH-LOGICAL-c617t-89999fd20b3a25c3bf84a8a0a81d416aca1ceb9d7ee979cf45855399bdbecf433</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/106/48.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/25593359$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/25593359$$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/19910535$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/1040276$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Evrin, Cecile</creatorcontrib><creatorcontrib>Clarke, Pippa</creatorcontrib><creatorcontrib>Zech, Juergen</creatorcontrib><creatorcontrib>Lurz, Rudi</creatorcontrib><creatorcontrib>Sun, Jingchuan</creatorcontrib><creatorcontrib>Uhle, Stefan</creatorcontrib><creatorcontrib>Li, Huilin</creatorcontrib><creatorcontrib>Stillman, Bruce</creatorcontrib><creatorcontrib>Speck, Christian</creatorcontrib><creatorcontrib>BROOKHAVEN NATIONAL LABORATORY (BNL)</creatorcontrib><title>double-hexameric MCM2-7 complex is loaded onto origin DNA during licensing of eukaryotic DNA replication</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>During pre-replication complex (pre-RC) formation, origin recognition complex (ORC), Cdc6, and Cdt1 cooperatively load the 6-subunit mini chromosome maintenance (MCM2-7) complex onto DNA. Loading of MCM2-7 is a prerequisite for DNA licensing that restricts DNA replication to once per cell cycle. During S phase MCM2-7 functions as part of the replicative helicase but within the pre-RC MCM2-7 is inactive. The organization of replicative DNA helicases before and after loading onto DNA has been studied in bacteria and viruses but not eukaryotes and is of major importance for understanding the MCM2-7 loading mechanism and replisome assembly. Lack of an efficient reconstituted pre-RC system has hindered the detailed mechanistic and structural analysis of MCM2-7 loading for a long time. We have reconstituted Saccharomyces cerevisiae pre-RC formation with purified proteins and showed efficient loading of MCM2-7 onto origin DNA in vitro. MCM2-7 loading was found to be dependent on the presence of all pre-RC proteins, origin DNA, and ATP hydrolysis. The quaternary structure of MCM2-7 changes during pre-RC formation: MCM2-7 before loading is a single hexamer in solution but is transformed into a double-hexamer during pre-RC formation. Using electron microscopy (EM), we observed that loaded MCM2-7 encircles DNA. The loaded MCM2-7 complex can slide on DNA, and sliding is not directional. Our results provide key insights into mechanisms of pre-RC formation and have important implications for understanding the role of the MCM2-7 in establishment of bidirectional replication forks.</description><subject>60 APPLIED LIFE SCIENCES</subject><subject>Animals</subject><subject>BACTERIA</subject><subject>BASIC BIOLOGICAL SCIENCES</subject><subject>Biological Sciences</subject><subject>CELL CYCLE</subject><subject>Chromatography, Gel</subject><subject>Chromosomal Proteins, Non-Histone - metabolism</subject><subject>CHROMOSOMES</subject><subject>Cloning, Molecular</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>DNA HELICASES</subject><subject>DNA Helicases - metabolism</subject><subject>DNA REPLICATION</subject><subject>DNA Replication - physiology</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>ELECTRON MICROSCOPY</subject><subject>Eukaryotes</subject><subject>helicase</subject><subject>HYDROLYSIS</subject><subject>IN VITRO</subject><subject>initiation</subject><subject>LICENSING</subject><subject>MAINTENANCE</subject><subject>Microscopy, Electron</subject><subject>mini chromosome maintenance</subject><subject>Models, Molecular</subject><subject>Molecular structure</subject><subject>Multiprotein Complexes - metabolism</subject><subject>Multiprotein Complexes - ultrastructure</subject><subject>Oligonucleotides</subject><subject>ORC</subject><subject>ORIGIN</subject><subject>Plasmids</subject><subject>pre-RC</subject><subject>Protein Conformation</subject><subject>PROTEINS</subject><subject>Replication origin</subject><subject>SACCHAROMYCES CEREVISIAE</subject><subject>Saccharomyces cerevisiae Proteins - metabolism</subject><subject>Salts</subject><subject>Viral tumor antigens</subject><subject>VIRUSES</subject><subject>Xenopus</subject><subject>Yeast</subject><subject>Yeasts</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1v1DAQhiMEokvhzAmwuCAOacexHccXpGpbPqQWDtCz5TjOrpesndoOWv49XmW1Cyd8sUfz-J15Z4riJYYLDJxcjk7FCxAYMwAM9aNigXNU1lTA42IBUPGyoRU9K57FuAEAwRp4WpxhITAwwhbFuvNTO5hybXZqa4LV6G55V5Ucab8dB7NDNqLBq850yLvkkQ92ZR26_nqFuilYt0KD1cbF_cv3yEw_VfjtU9bZI8GMOa2S9e558aRXQzQvDvd5cf_x5sfyc3n77dOX5dVtqWvMU9mIfPqugpaoimnS9g1VjQLV4I7iWmmFtWlFx40RXOiesoYxIkTbtSZHhJwXH2bdcWq3psu9paAGOQa7zZ1Jr6z8N-PsWq78L1nxhuOaZYG3s4CPycqobTJ6rb1zRieJgeaZ1hl6d6gS_MNkYpJbG7UZBuWMn6LkhGBSESZOckdy46fg8ghkBZhCzTjO0OUM6eBjDKY_9otB7hct94uWp0XnH6__tnniD5vNADoA-58nuVrSJleuKGTk_X8Q2U_DkMwuZfbVzG5i8uEIVyxbnG2-mfO98lKtgo3y_ns2SABzDA2tyR8vqM_D</recordid><startdate>20091201</startdate><enddate>20091201</enddate><creator>Evrin, Cecile</creator><creator>Clarke, Pippa</creator><creator>Zech, Juergen</creator><creator>Lurz, Rudi</creator><creator>Sun, Jingchuan</creator><creator>Uhle, Stefan</creator><creator>Li, Huilin</creator><creator>Stillman, Bruce</creator><creator>Speck, Christian</creator><general>National Academy of Sciences</general><general>National Acad Sciences</general><scope>FBQ</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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>OTOTI</scope><scope>5PM</scope></search><sort><creationdate>20091201</creationdate><title>double-hexameric MCM2-7 complex is loaded onto origin DNA during licensing of eukaryotic DNA replication</title><author>Evrin, Cecile ; Clarke, Pippa ; Zech, Juergen ; Lurz, Rudi ; Sun, Jingchuan ; Uhle, Stefan ; Li, Huilin ; Stillman, Bruce ; Speck, Christian</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c617t-89999fd20b3a25c3bf84a8a0a81d416aca1ceb9d7ee979cf45855399bdbecf433</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>60 APPLIED LIFE SCIENCES</topic><topic>Animals</topic><topic>BACTERIA</topic><topic>BASIC BIOLOGICAL SCIENCES</topic><topic>Biological Sciences</topic><topic>CELL CYCLE</topic><topic>Chromatography, Gel</topic><topic>Chromosomal Proteins, Non-Histone - metabolism</topic><topic>CHROMOSOMES</topic><topic>Cloning, Molecular</topic><topic>Deoxyribonucleic acid</topic><topic>DNA</topic><topic>DNA HELICASES</topic><topic>DNA Helicases - metabolism</topic><topic>DNA REPLICATION</topic><topic>DNA Replication - physiology</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>ELECTRON MICROSCOPY</topic><topic>Eukaryotes</topic><topic>helicase</topic><topic>HYDROLYSIS</topic><topic>IN VITRO</topic><topic>initiation</topic><topic>LICENSING</topic><topic>MAINTENANCE</topic><topic>Microscopy, Electron</topic><topic>mini chromosome maintenance</topic><topic>Models, Molecular</topic><topic>Molecular structure</topic><topic>Multiprotein Complexes - metabolism</topic><topic>Multiprotein Complexes - ultrastructure</topic><topic>Oligonucleotides</topic><topic>ORC</topic><topic>ORIGIN</topic><topic>Plasmids</topic><topic>pre-RC</topic><topic>Protein Conformation</topic><topic>PROTEINS</topic><topic>Replication origin</topic><topic>SACCHAROMYCES CEREVISIAE</topic><topic>Saccharomyces cerevisiae Proteins - metabolism</topic><topic>Salts</topic><topic>Viral tumor antigens</topic><topic>VIRUSES</topic><topic>Xenopus</topic><topic>Yeast</topic><topic>Yeasts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Evrin, Cecile</creatorcontrib><creatorcontrib>Clarke, Pippa</creatorcontrib><creatorcontrib>Zech, Juergen</creatorcontrib><creatorcontrib>Lurz, Rudi</creatorcontrib><creatorcontrib>Sun, Jingchuan</creatorcontrib><creatorcontrib>Uhle, Stefan</creatorcontrib><creatorcontrib>Li, Huilin</creatorcontrib><creatorcontrib>Stillman, Bruce</creatorcontrib><creatorcontrib>Speck, Christian</creatorcontrib><creatorcontrib>BROOKHAVEN NATIONAL LABORATORY (BNL)</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>OSTI.GOV</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>Evrin, Cecile</au><au>Clarke, Pippa</au><au>Zech, Juergen</au><au>Lurz, Rudi</au><au>Sun, Jingchuan</au><au>Uhle, Stefan</au><au>Li, Huilin</au><au>Stillman, Bruce</au><au>Speck, Christian</au><aucorp>BROOKHAVEN NATIONAL LABORATORY (BNL)</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>double-hexameric MCM2-7 complex is loaded onto origin DNA during licensing of eukaryotic DNA replication</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2009-12-01</date><risdate>2009</risdate><volume>106</volume><issue>48</issue><spage>20240</spage><epage>20245</epage><pages>20240-20245</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>During pre-replication complex (pre-RC) formation, origin recognition complex (ORC), Cdc6, and Cdt1 cooperatively load the 6-subunit mini chromosome maintenance (MCM2-7) complex onto DNA. Loading of MCM2-7 is a prerequisite for DNA licensing that restricts DNA replication to once per cell cycle. During S phase MCM2-7 functions as part of the replicative helicase but within the pre-RC MCM2-7 is inactive. The organization of replicative DNA helicases before and after loading onto DNA has been studied in bacteria and viruses but not eukaryotes and is of major importance for understanding the MCM2-7 loading mechanism and replisome assembly. Lack of an efficient reconstituted pre-RC system has hindered the detailed mechanistic and structural analysis of MCM2-7 loading for a long time. We have reconstituted Saccharomyces cerevisiae pre-RC formation with purified proteins and showed efficient loading of MCM2-7 onto origin DNA in vitro. MCM2-7 loading was found to be dependent on the presence of all pre-RC proteins, origin DNA, and ATP hydrolysis. The quaternary structure of MCM2-7 changes during pre-RC formation: MCM2-7 before loading is a single hexamer in solution but is transformed into a double-hexamer during pre-RC formation. Using electron microscopy (EM), we observed that loaded MCM2-7 encircles DNA. The loaded MCM2-7 complex can slide on DNA, and sliding is not directional. Our results provide key insights into mechanisms of pre-RC formation and have important implications for understanding the role of the MCM2-7 in establishment of bidirectional replication forks.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>19910535</pmid><doi>10.1073/pnas.0911500106</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | 60 APPLIED LIFE SCIENCES Animals BACTERIA BASIC BIOLOGICAL SCIENCES Biological Sciences CELL CYCLE Chromatography, Gel Chromosomal Proteins, Non-Histone - metabolism CHROMOSOMES Cloning, Molecular Deoxyribonucleic acid DNA DNA HELICASES DNA Helicases - metabolism DNA REPLICATION DNA Replication - physiology DNA-Binding Proteins - metabolism ELECTRON MICROSCOPY Eukaryotes helicase HYDROLYSIS IN VITRO initiation LICENSING MAINTENANCE Microscopy, Electron mini chromosome maintenance Models, Molecular Molecular structure Multiprotein Complexes - metabolism Multiprotein Complexes - ultrastructure Oligonucleotides ORC ORIGIN Plasmids pre-RC Protein Conformation PROTEINS Replication origin SACCHAROMYCES CEREVISIAE Saccharomyces cerevisiae Proteins - metabolism Salts Viral tumor antigens VIRUSES Xenopus Yeast Yeasts |
| title | double-hexameric MCM2-7 complex is loaded onto origin DNA during licensing of eukaryotic DNA replication |
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