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A novel human AP endonuclease with conserved zinc-finger-like motifs involved in DNA strand break responses.

Publication ,  Journal Article
Kanno, S-I; Kuzuoka, H; Sasao, S; Hong, Z; Lan, L; Nakajima, S; Yasui, A
Published in: EMBO J
April 18, 2007

DNA damage causes genome instability and cell death, but many of the cellular responses to DNA damage still remain elusive. We here report a human protein, PALF (PNK and APTX-like FHA protein), with an FHA (forkhead-associated) domain and novel zinc-finger-like CYR (cysteine-tyrosine-arginine) motifs that are involved in responses to DNA damage. We found that the CYR motif is widely distributed among DNA repair proteins of higher eukaryotes, and that PALF, as well as a Drosophila protein with tandem CYR motifs, has endo- and exonuclease activities against abasic site and other types of base damage. PALF accumulates rapidly at single-strand breaks in a poly(ADP-ribose) polymerase 1 (PARP1)-dependent manner in human cells. Indeed, PALF interacts directly with PARP1 and is required for its activation and for cellular resistance to methyl-methane sulfonate. PALF also interacts directly with KU86, LIGASEIV and phosphorylated XRCC4 proteins and possesses endo/exonuclease activity at protruding DNA ends. Various treatments that produce double-strand breaks induce formation of PALF foci, which fully coincide with gammaH2AX foci. Thus, PALF and the CYR motif may play important roles in DNA repair of higher eukaryotes.

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Published In

EMBO J

DOI

ISSN

0261-4189

Publication Date

April 18, 2007

Volume

26

Issue

8

Start / End Page

2094 / 2103

Location

England

Related Subject Headings

  • Zinc Fingers
  • Sequence Alignment
  • RNA, Small Interfering
  • Protein Structure, Tertiary
  • Poly-ADP-Ribose Binding Proteins
  • Poly(ADP-ribose) Polymerases
  • Poly (ADP-Ribose) Polymerase-1
  • Oligonucleotides
  • Molecular Sequence Data
  • Mice, Knockout
 

Citation

APA
Chicago
ICMJE
MLA
NLM
Kanno, S.-I., Kuzuoka, H., Sasao, S., Hong, Z., Lan, L., Nakajima, S., & Yasui, A. (2007). A novel human AP endonuclease with conserved zinc-finger-like motifs involved in DNA strand break responses. EMBO J, 26(8), 2094–2103. https://doi.org/10.1038/sj.emboj.7601663
Kanno, Shin-ichiro, Hiroyuki Kuzuoka, Shigeru Sasao, Zehui Hong, Li Lan, Satoshi Nakajima, and Akira Yasui. “A novel human AP endonuclease with conserved zinc-finger-like motifs involved in DNA strand break responses.EMBO J 26, no. 8 (April 18, 2007): 2094–2103. https://doi.org/10.1038/sj.emboj.7601663.
Kanno S-I, Kuzuoka H, Sasao S, Hong Z, Lan L, Nakajima S, et al. A novel human AP endonuclease with conserved zinc-finger-like motifs involved in DNA strand break responses. EMBO J. 2007 Apr 18;26(8):2094–103.
Kanno, Shin-ichiro, et al. “A novel human AP endonuclease with conserved zinc-finger-like motifs involved in DNA strand break responses.EMBO J, vol. 26, no. 8, Apr. 2007, pp. 2094–103. Pubmed, doi:10.1038/sj.emboj.7601663.
Kanno S-I, Kuzuoka H, Sasao S, Hong Z, Lan L, Nakajima S, Yasui A. A novel human AP endonuclease with conserved zinc-finger-like motifs involved in DNA strand break responses. EMBO J. 2007 Apr 18;26(8):2094–2103.

Published In

EMBO J

DOI

ISSN

0261-4189

Publication Date

April 18, 2007

Volume

26

Issue

8

Start / End Page

2094 / 2103

Location

England

Related Subject Headings

  • Zinc Fingers
  • Sequence Alignment
  • RNA, Small Interfering
  • Protein Structure, Tertiary
  • Poly-ADP-Ribose Binding Proteins
  • Poly(ADP-ribose) Polymerases
  • Poly (ADP-Ribose) Polymerase-1
  • Oligonucleotides
  • Molecular Sequence Data
  • Mice, Knockout