TERRA and hnRNPA1 orchestrate an RPA-to-POT1 switch on telomeric single-stranded DNA

Rachel Litman Flynn, Richard C. Centore, Roderick J. O’Sullivan, Rekha Rai, Alice Tse, Zhou Songyang, Sandy Chang, Jan Karlseder and Lee Zou ()
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Rachel Litman Flynn: Massachusetts General Hospital Cancer Center, Harvard Medical School
Richard C. Centore: Massachusetts General Hospital Cancer Center, Harvard Medical School
Roderick J. O’Sullivan: Molecular and Cellular Laboratory, The Salk Institute for Biological Studies
Rekha Rai: Yale University School of Medicine
Alice Tse: Massachusetts General Hospital Cancer Center, Harvard Medical School
Zhou Songyang: Baylor College of Medicine
Sandy Chang: Yale University School of Medicine
Jan Karlseder: Molecular and Cellular Laboratory, The Salk Institute for Biological Studies
Lee Zou: Massachusetts General Hospital Cancer Center, Harvard Medical School

Nature, 2011, vol. 471, issue 7339, 532-536

Abstract: POT1 and RPA go their separate ways Two single-stranded DNA binding proteins, POT1 and RPA, associate with the ends of DNA chromosomes, which are known as telomeres. Binding of RPA to telomeres can activate a DNA damage response, so it was suggested that POT1 might bind telomeres to prevent RPA association. Zou and colleagues unexpectedly find that POT1 and its partner TPP1 do not prevent RPA binding, but hnRNPA1 does. TERRA, a telomere-associated RNA, displaces hnRNPA1 and promotes POT1 binding after S phase, when replication is completed.

Date: 2011
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DOI: 10.1038/nature09772

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