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

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 rif1Δ, rif2Δ 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.

Pubmed ID: 22354040


  • Luciano P
  • Coulon S
  • Faure V
  • Corda Y
  • Bos J
  • Brill SJ
  • Gilson E
  • Simon MN
  • Géli V


The EMBO journal

Publication Data

April 18, 2012

Associated Grants


Mesh Terms

  • Chromosomes
  • Mutant Proteins
  • Mutation, Missense
  • Protein Binding
  • Protein Interaction Mapping
  • Replication Protein A
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Schizosaccharomyces
  • Telomerase
  • Telomere