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Single-molecule imaging brings Rad51 nucleoprotein filaments into focus.

Authors
Type
Published Article
Journal
Trends in Cell Biology
0962-8924
Publisher
Elsevier
Volume
20
Issue
5
Pages
269–276
Identifiers
DOI: 10.1016/j.tcb.2010.02.004
Source
Kowalczykowski Lab

Abstract

The Rad51 protein is essential for DNA repair by homologous recombination. After DNA damage, Rad51 localizes to nuclear foci that represent sites of DNA repair in vivo. In vitro, Rad51 self-assembles on single- or double-stranded DNA to form a nucleoprotein filament. Recently, the merging of innovative single-molecule techniques with ensemble methods has provided unique insights into the dynamic nature of this filament and its cellular function. The assembly and disassembly of Rad51 nucleoprotein filaments is seen to be regulated by recombination accessory proteins. In this regard, the BRC repeats of the BRCA2 protein were shown to modulate the DNA binding selectivity of Rad51. Furthermore, single-molecule studies explained the need for a DNA translocase, Rad54 protein, in the disassembly of Rad51 double-stranded DNA filaments.

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