Getting a grip on licensing: Mechanism of stable Mcm2-7 loading onto replication origins

被引：26

作者：

Cvetic, CA ^{[1
]}

Walter, JC ^{[1
]}

机构：

[1] Harvard Univ, Sch Med, Dept Biol Chem & Mol Pharmacol, Boston, MA 02446 USA

来源：

MOLECULAR CELL | 2006年 / 21卷 / 02期

关键词：

D O I：

10.1016/j.molcel.2006.01.003

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A recent Molecular Cell paper by Randell et al. (2006) sheds light on the role of ATP hydrolysis by Cdc6 in promoting the stable loading of the Mcm2-7 complex onto origins of DNA replication.

引用

页码：143 / 144

页数：2

共 6 条

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Bowers, JL ;

Randell, JCW ;

Chen, SY ;

Bell, SP .

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Cvetic, C ;

Gilbert, CH ;

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Walter, JC .

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[4] Sequential ATP hydrolysis by Cdc6 and ORC directs loading of the Mcm2-7 helicase [J].

Randell, JCW ;

Bowers, JL ;

Rodríguez, HK ;

Bell, SP .

MOLECULAR CELL, 2006, 21 (01) :29-39

[5] Pumps, paradoxes and ploughshares: mechanism of the MCM2-7 DNA helicase [J].

Takahashi, TS ;

Wigley, DB ;

Walter, JC .

TRENDS IN BIOCHEMICAL SCIENCES, 2005, 30 (08) :437-444

[6] The ATPase activity of MCM2-7 is dispensable for pre-RC assembly but is required for DNA unwinding [J].

Ying, CY ;

Gautier, J .

EMBO JOURNAL, 2005, 24 (24) :4334-4344

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