Functional and structural basis for a bacteriophage homolog of human RAD52.

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Serval ID
serval:BIB_2CCD57AED525
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Functional and structural basis for a bacteriophage homolog of human RAD52.
Journal
Current Biology
Author(s)
Ploquin M., Bransi A., Paquet E.R., Stasiak A.Z., Stasiak A., Yu X., Cieslinska A.M., Egelman E.H., Moineau S., Masson J.Y.
ISSN
0960-9822
Publication state
Published
Issued date
08/2008
Peer-reviewed
Oui
Volume
18
Number
15
Pages
1142-1146
Language
english
Abstract
In eukaryotes, homologous recombination proteins such as RAD51 and RAD52 play crucial roles in DNA repair and genome stability. Human RAD52 is a member of a large single-strand annealing protein (SSAP) family [1] and stimulates Rad51-dependent recombination [2, 3]. In prokaryotes and phages, it has been difficult to establish the presence of RAD52 homologs with conserved sequences. Putative SSAPs were recently found in several phages that infect strains of Lactococcus lactis[4]. One of these SSAPs was identified as Sak and was found in the virulent L. lactis phage ul36, which belongs to the Siphoviridae family [4, 5]. In this study, we show that Sak is homologous to the N terminus of human RAD52. Purified Sak binds single-stranded DNA (ssDNA) preferentially over double-stranded DNA (dsDNA) and promotes the renaturation of long complementary ssDNAs. Sak also binds RecA and stimulates homologous recombination reactions. Mutations shown to modulate RAD52 DNA binding [6] affect Sak similarly. Remarkably, electron-microscopic reconstruction of Sak reveals an undecameric (11) subunit ring, similar to the crystal structure of the N-terminal fragment of human RAD52 [7, 8]. For the first time, we propose a viral homolog of RAD52 at the amino acid, phylogenic, functional, and structural levels.
Keywords
Amino Acid Sequence, DNA Repair, DNA-Binding Proteins/chemistry, DNA-Binding Proteins/physiology, Humans, Lactococcus lactis/virology, Models, Molecular, Molecular Sequence Data, Phylogeny, Rad52 DNA Repair and Recombination Protein/chemistry, Rad52 DNA Repair and Recombination Protein/physiology, Sequence Alignment, Sequence Homology, Amino Acid, Siphoviridae/genetics, Structural Homology, Protein, Viral Proteins/chemistry, Viral Proteins/physiology
Pubmed
Web of science
Open Access
Yes
Create date
26/11/2008 16:54
Last modification date
20/08/2019 13:11
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