A double-hexameric MCM2-7 complex is loaded onto origin DNA during licensing of 
eukaryotic DNA replication.

Evrin, Cecile; Clarke, Pippa; Zech, Juergen; Lurz, Rudi; Sunc, Jingchuan; Uhle, Stefan; Li, Huilin; Stillman, Bruce; Speck, Christian

doi:10.1073/pnas.0911500106

A double-hexameric MCM2-7 complex is loaded onto origin DNA during licensing of eukaryotic DNA replication.

Evrin, C., Clarke, P., Zech, J., Lurz, R., Sunc, J., Uhle, S., Li, H., Stillman, B., & Speck, C. (2009). A double-hexameric MCM2-7 complex is loaded onto origin DNA during licensing of eukaryotic DNA replication. Proceedings of the National Academy of Sciences of the United States of America, 106(48), 20240--20245. doi:10.1073/pnas.0911500106.

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アイテムのパーマリンク: https://hdl.handle.net/11858/00-001M-0000-0010-7CBE-6 版のパーマリンク: https://hdl.handle.net/11858/00-001M-0000-0010-7CBF-4

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その他のタイトル : Proc. Natl. Acad. Sci. U S A

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Evrin, Cecile, 著者
Clarke, Pippa, 著者
Zech, Juergen, 著者
Lurz, Rudi¹, 著者
Sunc, Jingchuan, 著者
Uhle, Stefan, 著者
Li, Huilin, 著者
Stillman, Bruce, 著者
Speck, Christian, 著者

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1Max Planck Society, ou_persistent13

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要旨: 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.

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言語: eng - English

日付: 出版: 2009-12-01

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識別子（DOI, ISBNなど）: eDoc: 473602
URI: This article contains supporting information online at www.pnas.org/cgi/content/full/0911500106/DCSupplemental.
DOI: 10.1073/pnas.0911500106

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出版物名: Proceedings of the National Academy of Sciences of the United States of America

出版物の別名 : Proc. Natl. Acad. Sci. U S A

種別: 学術雑誌

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ページ: - 巻号: 106 (48) 通巻号: - 開始・終了ページ: 20240- - 20245 識別子（ISBN, ISSN, DOIなど）: ISSN: 0027-8424

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