期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 106, 期 46, 页码 19298-19303出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0909203106
关键词
end capping; Stn1; Ten1; Cdc13; t-RPA
资金
- National Science Foundation [0617956]
- University of Colorado Cancer Center Pilot Award
- National Institutes of Health (NIH) [GM083953]
- Mathers Charitable Foundation
- NIH Training Appointment [T32 GM-008732]
- Direct For Biological Sciences
- Div Of Molecular and Cellular Bioscience [0617956] Funding Source: National Science Foundation
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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据