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Mol Cell
2006 Mar 17;216:837-48. doi: 10.1016/j.molcel.2006.01.036.
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Condensin I interacts with the PARP-1-XRCC1 complex and functions in DNA single-strand break repair.
Heale JT
,
Ball AR
,
Schmiesing JA
,
Kim JS
,
Kong X
,
Zhou S
,
Hudson DF
,
Earnshaw WC
,
Yokomori K
.
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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.
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