Analysis of the mammalian recombination protein complex RC-1.
Based 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 epsilon. 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.
Jessberger
R
R
Basel Institute for Immunology, Switzerland.
Chui
G
G
Linn
S
S
Kemper
B
B
D001483:Base Sequence; D015153:Blotting, Western; D004247:DNA / Q000737:chemistry / Q000378:metabolism; D011088:DNA Ligases / Q000378:metabolism*; D004257:DNA Polymerase II; D004260:DNA Repair / Q000235:genetics*; D004259:DNA-Directed DNA Polymerase / Q000378:metabolism*; D003850:Deoxyribonuclease I / Q000378:metabolism*; D004706:Endodeoxyribonucleases / Q000378:metabolism*; D008957:Models, Genetic; D008969:Molecular Sequence Data; D009097:Multienzyme Complexes / Q000378:metabolism*; D009690:Nucleic Acid Conformation; D011995:Recombination, Genetic
D009097:Multienzyme Complexes; C101162:RC-1 recombination protein complex; D004247:DNA; D004257:DNA Polymerase II; D004259:DNA-Directed DNA Polymerase; D004706:Endodeoxyribonucleases; D003850:Deoxyribonuclease I; D011088:DNA Ligases