XRCC1 Polypeptide Interacts with DNA Polymerase and Possibly Poly (ADP-Ribose) Polymerase, and DNA Ligase III Is a Novel Molecular 'Nick-Sensor' In Vitro | Zendy

Keith W. Caldecott | Zendy; Saïd Aoufouchi | Zendy; Peter Johnson | Zendy; Sidney SHALL | Zendy

Open Access

XRCC1 Polypeptide Interacts with DNA Polymerase and Possibly Poly (ADP-Ribose) Polymerase, and DNA Ligase III Is a Novel Molecular 'Nick-Sensor' In Vitro

Author(s) -

Keith W. Caldecott,

Saïd Aoufouchi,

Peter Johnson,

Sidney SHALL

Publication year - 1996

Publication title -

nucleic acids research

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 9.008

H-Index - 537

eISSN - 1362-4954

pISSN - 0305-1048

DOI - 10.1093/nar/24.22.4387

Subject(s) - dna ligase , xrcc1 , biology , dna clamp , dna polymerase , dna polymerase mu , polymerase , poly adp ribose polymerase , dna polymerase ii , microbiology and biotechnology , dna repair , dna polymerase i , biochemistry , dna , polymerase chain reaction , circular bacterial chromosome , gene , reverse transcriptase , genotype , single nucleotide polymorphism

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.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research