RadA protein from Archaeoglobus fulgidus forms rings, nucleoprotein filaments and catalyses homologous recombination.

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Serval ID
serval:BIB_2AA943F89A26
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
RadA protein from Archaeoglobus fulgidus forms rings, nucleoprotein filaments and catalyses homologous recombination.
Journal
Nucleic Acids Research
Author(s)
McIlwraith M.J., Hall D.R., Stasiak A.Z., Stasiak A., Wigley D.B., West S.C.
ISSN
1362-4962[electronic], 0305-1048[linking]
Publication state
Published
Issued date
11/2001
Volume
29
Number
22
Pages
4509-4517
Language
english
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Abstract
Proteins that catalyse homologous recombination have been identified in all living organisms and are essential for the repair of damaged DNA as well as for the generation of genetic diversity. In bacteria homologous recombination is performed by the RecA protein, whereas in the eukarya a related protein called Rad51 is required to catalyse recombination and repair. More recently, archaeal homologues of RecA/Rad51 (RadA) have been identified and isolated. In this work we have cloned and purified the RadA protein from the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus and characterised its in vitro activities. We show that (i) RadA protein forms ring structures in solution and binds single- but not double-stranded DNA to form nucleoprotein filaments, (ii) RadA is a single-stranded DNA-dependent ATPase at elevated temperatures, and (iii) RadA catalyses efficient D-loop formation and strand exchange at temperatures of 60-70 degrees C. Finally, we have used electron microscopy to visualise RadA-mediated joint molecules, the intermediates of homologous recombination. Intriguingly, RadA shares properties of both the bacterial RecA and eukaryotic Rad51 recombinases.
Keywords
Adenosine Diphosphate/metabolism, Adenosine Triphosphatases/metabolism, Adenosine Triphosphate/metabolism, Archaeal Proteins/chemistry, Archaeal Proteins/genetics, Archaeoglobus fulgidus/chemistry, DNA/chemistry, DNA/metabolism, DNA, Single-Stranded/chemistry, DNA, Single-Stranded/metabolism, DNA-Binding Proteins/chemistry, DNA-Binding Proteins/genetics, Microscopy, Electron, Nucleic Acid Conformation, Nucleoproteins/chemistry, Nucleoproteins/metabolism, Protein Binding, Protein Conformation, Recombination, Genetic, Temperature
Pubmed
Web of science
Open Access
Yes
Create date
24/01/2008 11:36
Last modification date
25/09/2019 7:08
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