ATP-dependent structural change of the eukaryotic clamp-loader protein, replication factor C

被引:65
作者
Shiomi, Y
Usukura, J
Masamura, Y
Takeyasu, K
Nakayama, Y
Obuse, C
Yoshikawa, H
Tsurimoto, T [1 ]
机构
[1] Nara Inst Sci & Technol, Nara 6300101, Japan
[2] Nagoya Univ, Sch Med, Dept Anat, Nagoya, Aichi 4660065, Japan
[3] Kyoto Univ, Grad Sch Biostudies, Lab Plasma Membrane & Nucl Signaling, Kyoto 6068591, Japan
[4] Univ Osaka Prefecture, Dept Phys & Elect, Osaka 5998531, Japan
关键词
D O I
10.1073/pnas.97.26.14127
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The eukaryotic DNA sliding clamp that keeps DNA polymerase engaged at a replication fork, called proliferating cell nuclear antigen (PCNA), is loaded onto the 3' ends of primer DNA through its interaction with a heteropentameric protein complex called replication factor C (RFC). The ATPase activity of RFC is necessary for formation of a functional PCNA clamp. In the present study, the sensitivity of RFC to partial proteolysis is used to show that addition of ATP, ATP gammaS, or ADP induces different structural changes in RFC. Direct observation by electron microscopy reveals that RFC has a closed two-finger structure called the U form in the absence of ATP. This is converted into a more open C form on addition of ATP. in contrast, the structural changes induced by ATP gammaS or ADP are limited. These results suggest that RFC adapts on opened configuration intermediately after ATP hydrolysis. We further observe that PCNA is held between the two fingers of RFC and propose that the RFC structure change we observe during ATP hydrolysis causes the attached PCNA to form its active ring-like clamp on DNA.
引用
收藏
页码:14127 / 14132
页数:6
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