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TIMELESS Forms a Complex with PARP1 Distinct from Its Complex with TIPIN and Plays a Role in the DNA Damage Response.

Abstract：

:PARP1 is the main sensor of single- and double-strand breaks in DNA and, in building chains of poly(ADP-ribose), promotes the recruitment of many downstream signaling and effector proteins involved in the DNA damage response (DDR). We show a robust physical interaction between PARP1 and the replication fork protein TIMELESS, distinct from the known TIMELESS-TIPIN complex, which activates the intra-S phase checkpoint. TIMELESS recruitment to laser-induced sites of DNA damage is dependent on its binding to PARP1, but not PARP1 activity. We also find that the PARP1-TIMELESS complex contains a number of established PARP1 substrates, and TIMELESS mutants unable to bind PARP1 are impaired in their ability to bind PARP1 substrates. Further, PARP1 binding to certain substrates and their recruitment to DNA damage lesions is impaired by TIMELESS knockdown, and TIMELESS silencing significantly impairs DNA double-strand break repair. We hypothesize that TIMELESS cooperates in the PARP1-mediated DDR.

journal_name

Cell Rep

journal_title

Cell reports

authors

Young LM,Marzio A,Perez-Duran P,Reid DA,Meredith DN,Roberti D,Star A,Rothenberg E,Ueberheide B,Pagano M

doi

10.1016/j.celrep.2015.09.017

subject

Has Abstract

pub_date

2015-10-20 00:00:00

pages

451-459

issue

3

issn

2211-1247

pii

S2211-1247(15)01028-1

journal_volume

13

pub_type

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