title: Structure of a filament of stacked octamers of human DMC1 recombinase.
abstract: Eukaryal DMC1 proteins play a central role in homologous recombination in meiosis by assembling at the sites of programmed DNA double-strand breaks and carrying out a search for allelic DNA sequences located on homologous chromatids. They are close homologs of eukaryal Rad51 and archaeal RadA proteins and are remote homologs of bacterial RecA proteins. These recombinases (also called DNA strand-exchange proteins) promote a pivotal strand-exchange reaction between homologous single-stranded and double-stranded DNA substrates. An octameric form of a truncated human DMC1 devoid of its small N-terminal domain (residues 1-83) has been crystallized. The structure of the truncated DMC1 octamer is similar to that of the previously reported full-length DMC1 octamer, which has disordered N-terminal domains. In each protomer, only the ATP cap regions (Asp317-Glu323) show a noticeable conformational difference. The truncated DMC1 octamers further stack with alternate polarity into a filament. Similar filamentous assemblies of DMC1 have been observed to form on DNA by electron microscopy.
authors.affiliation: Department of Biochemistry, University of Saskatchewan, 107 Wiggins Road Suite A3, Saskatoon, Sasktchewan S7N 5E5, Canada.
authors.forename: Liqin
authors.initials: L
authors.lastname: Du
authors.forename: Yu
authors.initials: Y
authors.lastname: Luo
mesh_terms: D018797:Cell Cycle Proteins / Q000737:chemistry* / Q000648:ultrastructure; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000648:ultrastructure; D006801:Humans; D008854:Microscopy, Electron; D008958:Models, Molecular; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary
chemical_list: D018797:Cell Cycle Proteins; D004268:DNA-Binding Proteins; C074556:DMC1 protein, human
keywords: DMC1 proteins; DNA strand-exchange proteins; recombinases
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