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...

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Bibliographic Details
Published in:Molecular cell 2006-03, Vol.21 (6), p.837-848
Main Authors: Heale, Jason T., Ball, Alexander R., Schmiesing, John A., Kim, Jong-Soo, Kong, Xiangduo, Zhou, Sharleen, Hudson, Damien F., Earnshaw, William C., Yokomori, Kyoko
Format: Article
Language:English
Subjects:
Adenosine Triphosphatases - metabolism
Adenosine Triphosphatases - physiology
Animals
Animals, Genetically Modified
Carrier Proteins
Cell Cycle Proteins
Cell Line
Chickens - genetics
Chromatin
Chromosomal Proteins, Non-Histone
DNA
DNA Damage
DNA Repair
DNA, Single-Stranded
DNA-Binding Proteins - metabolism
DNA-Binding Proteins - physiology
HeLa Cells
Humans
Interphase
Mass Spectrometry
Mice - genetics
Mice, Knockout
Models, Biological
Multiprotein Complexes - metabolism
Multiprotein Complexes - physiology
Nuclear Proteins
Poly(ADP-ribose) Polymerases - genetics
Poly(ADP-ribose) Polymerases - metabolism
Poly(ADP-ribose) Polymerases - physiology
Transfection
X-ray Repair Cross Complementing Protein 1
Xenopus Proteins
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Summary: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 δ/ɛ 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.
ISSN:1097-2765
1097-4164
DOI:10.1016/j.molcel.2006.01.036