Telomere capping proteins are structurally related to RPA with an additional telomere-specific domain

被引：59

作者：

Gelinas, Amy D. ^{[1
]}

Paschini, Margherita ^{[2
,3
]}

Reyes, Francis E. ^{[1
]}

Heroux, Annie ^{[4
]}

Batey, Robert T. ^{[1
]}

Lundblad, Victoria ^{[2
]}

Wuttke, Deborah S. ^{[1
]}

机构：

[1] Univ Colorado, Dept Chem & Biochem, Boulder, CO 80309 USA

[2] Salk Inst Biol Studies, Mol & Cell Biol Lab, La Jolla, CA 92037 USA

[3] Univ Calif San Diego, Div Biol Sci, La Jolla, CA USA

[4] Brookhaven Natl Lab, Dept Biol, Upton, NY 11973 USA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2009年 / 106卷 / 46期

基金：

美国国家卫生研究院; 美国国家科学基金会;

关键词：

end capping; Stn1; Ten1; Cdc13; t-RPA; SINGLE-STRANDED-DNA; CRYSTAL-STRUCTURE; END PROTECTION; BINDING; RECOGNITION; MUTANTS; COMPLEX; STN1; POT1; ASSOCIATION;

D O I：

10.1073/pnas.0909203106

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：

Telomeres must be capped to preserve chromosomal stability. The conserved Stn1 and Ten1 proteins are required for proper capping of the telomere, although the mechanistic details of how they contribute to telomere maintenance are unclear. Here, we report the crystal structures of the C-terminal domain of the Saccharomyces cerevisiae Stn1 and the Schizosaccharomyces pombe Ten1 proteins. These structures reveal striking similarities to corresponding subunits in the replication protein A complex, further supporting an evolutionary link between telomere maintenance proteins and DNA repair complexes. Our structural and in vivo data of Stn1 identify a new domain that has evolved to support a telomere-specific role in chromosome maintenance. These findings endorse a model of an evolutionarily conserved mechanism of DNA maintenance that has developed as a result of increased chromosomal structural complexity.

引用

页码：19298 / 19303

页数：6

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