Document Type
Article
Publication Date
1-1-2005
Publication Title
Nucleic Acids Research
Department
Geisel School of Medicine
Abstract
Homologous recombination provides an effective way to repair DNA double-strand breaks (DSBs) and is required for genetic recombination. During the process of homologous recombination, a heteroduplex DNA structure, or a ‘Holliday junction’ (HJ), is formed. The movement, or branch migration, of this junction is necessary for recombination to proceed correctly. In prokaryotes, the RecQ protein or the RuvA/RuvB protein complex can promote ATP-dependent branch migration of Holliday junctions. Much less is known about the processing of Holliday junctions in eukaryotes. Here, we identify RecQL1 as a predominant ATP-dependent, HJ branch migrator present in human nuclear extracts. A reduction in the level of RecQL1 induced by RNA interference in HeLa cells leads to an increase in sister chromatid exchange. We propose that RecQL1 is involved in the processing of Holliday junctions in human cells.
DOI
10.1093/nar/gki929
Dartmouth Digital Commons Citation
LeRoy, Gary; Carroll, Robert; Kyin, Saw; Seki, Masayuki; and Cole, Michael D., "Identification of RecQL1 as a Holliday Junction Processing Enzyme in Human Cell Lines" (2005). Dartmouth Scholarship. 3812.
https://digitalcommons.dartmouth.edu/facoa/3812
