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APE2 Zf-GRF facilitates 3′-5′ resection of DNA damage following oxidative stress

Wallace, Bret D. ; Berman, Zachary ; Mueller, Geoffrey A. ; Lin, Yunfeng ; Chang, Timothy ; Andres, Sara N. ; Wojtaszek, Jessica L. ; DeRose, Eugene F. ; Appel, C. Denise ; London, Robert E. ; Yan, Shan ; Williams, R. Scott

Proceedings of the National Academy of Sciences - PNAS, 2017-01, Vol.114 (2), p.304-309 [Periódico revisado por pares]

United States: National Academy of Sciences

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Título:
APE2 Zf-GRF facilitates 3′-5′ resection of DNA damage following oxidative stress
Autor: Wallace, Bret D. ; Berman, Zachary ; Mueller, Geoffrey A. ; Lin, Yunfeng ; Chang, Timothy ; Andres, Sara N. ; Wojtaszek, Jessica L. ; DeRose, Eugene F. ; Appel, C. Denise ; London, Robert E. ; Yan, Shan ; Williams, R. Scott
Assuntos: Animals ; APE2 ; BASIC BIOLOGICAL SCIENCES ; Binding sites ; Biological Sciences ; Chromatin ; crystallography ; DNA damage ; DNA Damage - genetics ; DNA Glycosylases - metabolism ; DNA Repair - genetics ; DNA Topoisomerases, Type I - metabolism ; DNA-(Apurinic or Apyrimidinic Site) Lyase - metabolism ; Endonucleases - metabolism ; Frogs ; Mutation ; oxidative stress ; Oxidative Stress - genetics ; Protein Domains - genetics ; Proteins ; Xenopus laevis ; Xenopus laevis - genetics ; Xenopus laevis - metabolism ; Zf-GRF
É parte de: Proceedings of the National Academy of Sciences - PNAS, 2017-01, Vol.114 (2), p.304-309
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
Univ. of North Carolina at Charlotte
National Inst. of General Medical Sciences of the National Inst. of Health (NIH)
W-31-109-Eng-38; R15 GM101571; R15 GM114713; R01 GM105404; 1Z01ES102765; 1Z01ES050111
USDOE Office of Science (SC), Basic Energy Sciences (BES)
USDOE Office of Science (SC), Biological and Environmental Research (BER)
1B.D.W. and Z.B. contributed equally to this work.
Edited by James E. Haber, Brandeis University, Waltham, MA, and approved December 1, 2016 (received for review June 21, 2016)
Author contributions: B.D.W., Z.B., G.A.M., J.L.W., C.D.A., S.Y., and R.S.W. designed research; B.D.W., Z.B., G.A.M., Y.L., T.C., S.N.A., J.L.W., E.F.D., and C.D.A. performed research; B.D.W., Z.B., G.A.M., Y.L., T.C., S.N.A., J.L.W., E.F.D., C.D.A., R.E.L., S.Y., and R.S.W. analyzed data; and S.Y. and R.S.W. wrote the paper.
Descrição: The Xenopus laevis APE2 (apurinic/apyrimidinic endonuclease 2) nuclease participates in 3′-5′ nucleolytic resection of oxidative DNA damage and activation of the ATR-Chk1 DNA damage response (DDR) pathway via ill-defined mechanisms. Here we report that APE2 resection activity is regulated by DNA interactions in its Zf-GRF domain, a region sharing high homology with DDR proteins Topoisomerase 3α (TOP3α) and NEIL3 (Nei-like DNA glycosylase 3), as well as transcription and RNA regulatory proteins, such as TTF2 (transcription termination factor 2), TFIIS, and RPB9. Biochemical and NMR results establish the nucleic acid-binding activity of the Zf-GRF domain. Moreover, an APE2 Zf-GRF X-ray structure and small-angle X-ray scattering analyses show that the Zf-GRF fold is typified by a crescent-shaped ssDNA binding claw that is flexibly appended to an APE2 endonuclease/exonuclease/phosphatase (EEP) catalytic core. Structure-guided Zf-GRF mutations impact APE2 DNA binding and 3′-5′ exonuclease processing, and also prevent efficient APE2-dependent RPA recruitment to damaged chromatin and activation of the ATR-Chk1 DDR pathway in response to oxidative stress in Xenopus egg extracts. Collectively, our data unveil the APE2 Zf-GRF domain as a nucleic acid interaction module in the regulation of a key single-strand break resection function of APE2, and also reveal topologic similarity of the Zf-GRF to the zinc ribbon domains of TFIIS and RPB9.
Editor: United States: National Academy of Sciences
Idioma: Inglês

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APE2 Zf-GRF facilitates 3′-5′ resection of DNA damage following oxidative stress

Wallace, Bret D. ; Berman, Zachary ; Mueller, Geoffrey A. ; Lin, Yunfeng ; Chang, Timothy ; Andres, Sara N. ; Wojtaszek, Jessica L. ; DeRose, Eugene F. ; Appel, C. Denise ; London, Robert E. ; Yan, Shan ; Williams, R. Scott

United States: National Academy of Sciences

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