Abstract
The DNA repair proteins XRCC1 and DNA ligase III are physically associated in human cells and directly interact in vitro and in vivo. Here, we demonstrate that XRCC1 is additionally associated with DNA polymerase-beta in human cells and that these polypeptides also directly interact. We also present data suggesting that poly (ADP-ribose) polymerase can interact with XRCC1. Finally, we demonstrate that DNA ligase III shares with poly (ADP-ribose) polymerase the novel function of a molecular DNA nick-sensor, and that the DNA ligase can inhibit activity of the latter polypeptide in vitro. Taken together, these data suggest that the activity of the four polypeptides described above may be co-ordinated in human cells within a single multiprotein complex.
MeSH Terms
Base Sequence
DNA Ligase ATP
DNA Ligases/chemistry,genetics,metabolism
DNA Polymerase I/chemistry,genetics,metabolism
DNA Repair
DNA-Binding Proteins/metabolism
Electrophoresis, Polyacrylamide Gel
Humans
Molecular Sequence Data
Poly(ADP-ribose) Polymerases/metabolism
Poly-ADP-Ribose Binding Proteins
X-ray Repair Cross Complementing Protein 1
Xenopus Proteins
Zinc Fingers
Chemicals
DNA-Binding Proteins
Poly-ADP-Ribose Binding Proteins
X-ray Repair Cross Complementing Protein 1
XRCC1 protein, human
Xenopus Proteins
Poly(ADP-ribose) Polymerases
DNA Polymerase I
DNA Ligases
DNA Ligase ATP
DNA ligase III alpha protein, Xenopus
LIG3 protein, human
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Caldecott K W
Zeneca Laboratory for Cell and Molecular Biology, School of Biological Sciences, University of Manchester, UK.
[email protected]
Aoufouchi S
Johnson P
Shall S
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