TY - JOUR
T1 - RPA-like proteins mediate yeast telomere function
AU - Gao, Hua
AU - Cervantes, Rachel B.
AU - Mandell, Edward K.
AU - Otero, Joel H.
AU - Lundblad, Victoria
N1 - Funding Information:
We thank the Brill (Rutgers University), Elledge (Harvard Medical School) and Wold (University of Iowa) laboratories for gifts of strains and plasmids, D. Wuttke and M. Wold for scientific conversations and advice, and E. Ford for technical assistance. This research was supported by Department of Defense postdoctoral fellowship DAMD 17-02-1-0276 (to R.B.C.), by grant GM55867 from the US National Institutes of Health and by the Lebensfeld Foundation.
PY - 2007/3
Y1 - 2007/3
N2 - Cdc13, Stn1 and Ten1 are essential yeast proteins that both protect chromosome termini from unregulated resection and regulate telomere length. Cdc13, which localizes to telomeres through high-affinity binding to telomeric single-stranded DNA, has been extensively characterized, whereas the contribution(s) of the Cdc13-associated Stn1 and Ten1 proteins to telomere function have remained unclear. We show here that Stn1 and Ten1 are DNA-binding proteins with specificity for telomeric DNA substrates. Furthermore, Stn1 and Ten1 show similarities to Rpa2 and Rpa3, subunits of the heterotrimeric replication protein A (RPA) complex, which is the major single-stranded DNA-binding activity in eukaryotic cells. We propose that Cdc13, Stn1 and Ten1 function as a telomere-specific RPA-like complex. Identification of an RPA-like complex that is targeted to a specific region of the genome suggests that multiple RPA-like complexes have evolved, each making individual contributions to genomic stability.
AB - Cdc13, Stn1 and Ten1 are essential yeast proteins that both protect chromosome termini from unregulated resection and regulate telomere length. Cdc13, which localizes to telomeres through high-affinity binding to telomeric single-stranded DNA, has been extensively characterized, whereas the contribution(s) of the Cdc13-associated Stn1 and Ten1 proteins to telomere function have remained unclear. We show here that Stn1 and Ten1 are DNA-binding proteins with specificity for telomeric DNA substrates. Furthermore, Stn1 and Ten1 show similarities to Rpa2 and Rpa3, subunits of the heterotrimeric replication protein A (RPA) complex, which is the major single-stranded DNA-binding activity in eukaryotic cells. We propose that Cdc13, Stn1 and Ten1 function as a telomere-specific RPA-like complex. Identification of an RPA-like complex that is targeted to a specific region of the genome suggests that multiple RPA-like complexes have evolved, each making individual contributions to genomic stability.
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U2 - 10.1038/nsmb1205
DO - 10.1038/nsmb1205
M3 - Article
C2 - 17293872
AN - SCOPUS:33847675342
SN - 1545-9993
VL - 14
SP - 208
EP - 214
JO - Nature Structural and Molecular Biology
JF - Nature Structural and Molecular Biology
IS - 3
ER -