Analysis of the mammalian recombination protein complex RC-1
1996; Elsevier BV; Volume: 350; Issue: 1 Linguagem: Inglês
10.1016/0027-5107(95)00106-9
ISSN1873-135X
AutoresRolf Jessberger, Gloria Chui, Stuart Linn, Börries Kemper,
Tópico(s)PARP inhibition in cancer therapy
ResumoBased on a novel cell-free assay for DNA recombination, we previously reported the purification and initial characterization of RC-1, a protein complex catalyzing the recombinational repair of deletions and gaps. RC-1 was isolated from calf thymus nuclear extracts and shown to copurify with several enzymatic activities, among them a DNA polymerase. Here, additional evidence is reported identifying the polymerase as DNA polymerase ϵ. Furthermore, a novel DNA structure-dependent endonuclease associated with RC-1 was observed, which recognizes and cleaves branched DNA substrates at specific sites. Implications of this endonuclease activity for the recombination reaction are discussed.
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