Condensin I interacts with the PARP-1-XRCC1 complex and functions in DNA single-strand break repair.

Condensins are essential protein complexes critical for mitotic chromosome organization. Little is known about the function of condensins during interphase, particularly in mammalian cells. Here we report the interphase-specific interaction between condensin I and the DNA nick-sensor poly(ADP-ribose) polymerase 1 (PARP-1). We show that the association between condensin I, PARP-1, ...
and the base excision repair (BER) factor XRCC1 increases dramatically upon single-strand break damage (SSB) induction. Damage-specific association of condensin I with the BER factors flap endonuclease 1 (FEN-1) and DNA polymerase delta/epsilon was also observed, suggesting that condensin I is recruited to interact with BER factors at damage sites. Consistent with this, DNA damage rapidly stimulates the chromatin association of PARP-1, condensin I, and XRCC1. Furthermore, depletion of condensin in vivo compromises SSB but not double-strand break (DSB) repair. Our results identify a SSB-specific response of condensin I through PARP-1 and demonstrate a role for condensin in SSB repair.
Mesh Terms:
Adenosine Triphosphatases, Animals, Animals, Genetically Modified, Carrier Proteins, Cell Line, Chickens, Chromatin, Chromosomal Proteins, Non-Histone, DNA Damage, DNA Repair, DNA, Single-Stranded, DNA-Binding Proteins, Hela Cells, Humans, Interphase, Mass Spectrometry, Mice, Mice, Knockout, Models, Biological, Multiprotein Complexes, Nuclear Proteins, Poly(ADP-ribose) Polymerases, Transfection, Xenopus Proteins
Mol. Cell
Date: Mar. 17, 2006
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