3k10
From Proteopedia
Crystal structure of telomere capping protein Stn1 from Saccharomyces cerevisiae
Structural highlights
FunctionSTN1_YEAST Has a role in telomere length regulation and telomere end protection. Acts as an inhibitor of telomerase loading through its interaction with CDC13.[1] [2] Publication Abstract from PubMedTelomeres 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. Telomere capping proteins are structurally related to RPA with an additional telomere-specific domain.,Gelinas AD, Paschini M, Reyes FE, Heroux A, Batey RT, Lundblad V, Wuttke DS Proc Natl Acad Sci U S A. 2009 Nov 17;106(46):19298-303. Epub 2009 Nov 2. PMID:19884503[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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