The Mechanism of ATP-Dependent Primer-Template Recognition by a Clamp Loader Complex

被引:103
作者
Simonetta, Kyle R. [1 ]
Kazmirski, Steven L. [1 ]
Goedken, Eric R. [1 ]
Cantor, Aaron J. [1 ]
Kelch, Brian A. [1 ]
McNally, Randall [1 ]
Seyedin, Steven N. [1 ]
Makino, Debora L. [1 ]
O'Donnell, Mike [3 ]
Kuriyan, John [1 ,2 ]
机构
[1] Univ Calif Berkeley, Howard Hughes Med Inst, Dept Chem, Dept Mol & Cell Biol, Berkeley, CA 94720 USA
[2] Univ Calif Berkeley, Lawrence Berkeley Lab, Phys Biosci Div, Berkeley, CA 94720 USA
[3] Rockefeller Univ, Howard Hughes Med Inst, New York, NY 10021 USA
关键词
DNA-POLYMERASE-III; REPLICATION FACTOR-C; CELL NUCLEAR ANTIGEN; ESCHERICHIA-COLI SSB; CRYSTAL-STRUCTURE; SLIDING CLAMP; GAMMA-COMPLEX; DELTA-SUBUNIT; STRUCTURAL-ANALYSIS; ACCESSORY PROTEINS;
D O I
10.1016/j.cell.2009.03.044
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
Clamp loaders load sliding clamps onto primer-template DNA. The structure of the E. coli clamp loader bound to DNA reveals the formation of an ATP-dependent spiral of ATPase domains that tracks only the template strand, allowing recognition of both RNA and DNA primers. Unlike hexameric helicases, in which DNA translocation requires distinct conformations of the ATPase domains, the clamp loader spiral is symmetric and is set up to trigger release upon DNA recognition. Specificity for primed DNA arises from blockage of the end of the primer and accommodation of the emerging template along a surface groove. A related structure reveals how the c protein, essential for coupling the clamp loader to single-stranded DNA-binding protein (SSB), binds to the clamp loader. By stabilizing a conformation of the clamp loader that is consistent with the ATPase spiral observed upon DNA binding, c binding promotes the clamp-loading activity of the complex.
引用
收藏
页码:659 / 671
页数:13
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