Tetrameric Ctp1 coordinates DNA binding and DNA bridging in DNA double-strand-break repair

Andres, Sara N.; Appel, C. Denise; Westmoreland, James W.; Williams, Jessica S.; Nguyen, Yvonne; Robertson, Patrick D.; Resnick, Michael A.; Williams, R. Scott

doi:10.1038/nsmb.2945

Title: Tetrameric Ctp1 coordinates DNA binding and DNA bridging in DNA double-strand-break repair

Journal Article · Mon Jan 12 00:00:00 EST 2015 · Nature Structural & Molecular Biology

DOI:https://doi.org/10.1038/nsmb.2945· OSTI ID:1247334

Andres, Sara N. ^[1]; Appel, C. Denise ^[1]; Westmoreland, James W. ^[1]; Williams, Jessica S. ^[1]; Nguyen, Yvonne ^[1]; Robertson, Patrick D. ^[1]; Resnick, Michael A. ^[1]; Williams, R. Scott ^[1]

Dept. of Health and Human Services (HHS), Research Triangle Park, NC (United States). National Inst. of Health. National Inst. of Environmental Health Sciences. Genome Integrity and Structural Biology Lab.

Ctp1 (also known as CtIP or Sae2) collaborates with Mre11-Rad50-Nbs1 to initiate repair of DNA double-strand breaks (DSBs), but its functions remain enigmatic. In this paper, we report that tetrameric Schizosaccharomyces pombe Ctp1 contains multivalent DNA-binding and DNA-bridging activities. Through structural and biophysical analyses of the Ctp1 tetramer, we define the salient features of Ctp1 architecture: an N-terminal interlocking tetrameric helical dimer-of-dimers (THDD) domain and a central intrinsically disordered region (IDR) linked to C-terminal 'RHR' DNA-interaction motifs. The THDD, IDR and RHR are required for Ctp1 DNA-bridging activity in vitro, and both the THDD and RHR are required for efficient DSB repair in S. pombe. Finally, our results establish non-nucleolytic roles of Ctp1 in binding and coordination of DSB-repair intermediates and suggest that ablation of human CtIP DNA binding by truncating mutations underlie the CtIP-linked Seckel and Jawad syndromes.

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Research Organization:: Dept. of Health and Human Services (HHS), Research Triangle Park, NC (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES); National Inst. of Health (NIH) (United States)

Grant/Contract Number:: W-31-109-Eng-38; 1Z01ES102765; 1Z01ES021016

OSTI ID:: 1247334

Journal Information:: Nature Structural & Molecular Biology, Vol. 22, Issue 2; ISSN 1545-9993

Publisher:: Nature Publishing GroupCopyright Statement

Country of Publication:: United States

Language:: ENGLISH

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Cited by: 47 works

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