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RPA facilitates telomerase activity at chromosome ends in budding and fission yeasts.


ABSTRACT: In Saccharomyces cerevisiae, the telomerase complex binds to chromosome ends and is activated in late S-phase through a process coupled to the progression of the replication fork. Here, we show that the single-stranded DNA-binding protein RPA (replication protein A) binds to the two daughter telomeres during telomere replication but only its binding to the leading-strand telomere depends on the Mre11/Rad50/Xrs2 (MRX) complex. We further demonstrate that RPA specifically co-precipitates with yKu, Cdc13 and telomerase. The interaction of RPA with telomerase appears to be mediated by both yKu and the telomerase subunit Est1. Moreover, a mutation in Rfa1 that affects both the interaction with yKu and telomerase reduces the dramatic increase in telomere length of a rif1?, rif2? double mutant. Finally, we show that the RPA/telomerase association and function are conserved in Schizosaccharomyces pombe. Our results indicate that in both yeasts, RPA directly facilitates telomerase activity at chromosome ends.

SUBMITTER: Luciano P 

PROVIDER: S-EPMC3343328 | biostudies-literature | 2012 Apr

REPOSITORIES: biostudies-literature

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RPA facilitates telomerase activity at chromosome ends in budding and fission yeasts.

Luciano Pierre P   Coulon Stéphane S   Faure Virginie V   Corda Yves Y   Bos Julia J   Brill Steven J SJ   Gilson Eric E   Simon Marie-Noelle MN   Géli Vincent V  

The EMBO journal 20120221 8


In Saccharomyces cerevisiae, the telomerase complex binds to chromosome ends and is activated in late S-phase through a process coupled to the progression of the replication fork. Here, we show that the single-stranded DNA-binding protein RPA (replication protein A) binds to the two daughter telomeres during telomere replication but only its binding to the leading-strand telomere depends on the Mre11/Rad50/Xrs2 (MRX) complex. We further demonstrate that RPA specifically co-precipitates with yKu,  ...[more]

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