期刊
CELL RESEARCH
卷 27, 期 12, 页码 1503-1520出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/cr.2017.145
关键词
telomere; shelterin; hub; TRFH; evolution
类别
资金
- Ministry of Science and Technology of China [2013CB910402]
- National Natural Science Foundation of China [31330040, 31525007, 31500625, 31470737, 31670748]
- Chinese Academy of Sciences [XDB08010201]
- Shanghai Science and Technology Commission [14JC1407200]
- Chinese Academy of Sciences
- Japan Society for the Promotion of Science (JSPS) KAKENHI [17H03606]
- Grants-in-Aid for Scientific Research [17H03606] Funding Source: KAKEN
Telomeric shelterin complex caps chromosome ends and plays a crucial role in telomere maintenance and protection. In the fission yeast Schizosaccharomyces pombe, shelterin is composed of telomeric single-and double-stranded DNA-binding protein subcomplexes Pot1-Tpz1 and Taz1-Rap1, which are bridged by their interacting protein Poz1. However, the structure of Poz1 and how Poz1 functions as an interaction hub in the shelterin complex remain unclear. Here we report the crystal structure of Poz1 in complex with Poz1-binding motifs of Tpz1 and Rap1. The crystal structure shows that Poz1 employs two different binding surfaces to interact with Tpz1 and Rap1. Unexpectedly, the structure also reveals that Poz1 adopts a dimeric conformation. Mutational analyses suggest that proper interactions between Tpz1, Poz1, and Rap1 in the shelterin core complex are required for telomere length homeostasis and heterochromatin structure maintenance at telomeres. Structural resemblance between Poz1 and the TRFH domains of other shelterin proteins in fission yeast and humans suggests a model for the evolution of shelterin proteins.
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