The E.coli RuvAB proteins branch migrate Holliday junctions through heterologous DNA sequences in a reaction facilitated by SSB.

Détails

ID Serval
serval:BIB_29E8A2A1B480
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
The E.coli RuvAB proteins branch migrate Holliday junctions through heterologous DNA sequences in a reaction facilitated by SSB.
Périodique
EMBO Journal
Auteur⸱e⸱s
Parsons C.A., Stasiak A., West S.C.
ISSN
0261-4189[print], 0261-4189[linking]
Statut éditorial
Publié
Date de publication
11/1995
Volume
14
Numéro
22
Pages
5736-5744
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Résumé
During genetic recombination a heteroduplex joint is formed between two homologous DNA molecules. The heteroduplex joint plays an important role in recombination since it accommodates sequence heterogeneities (mismatches, insertions or deletions) that lead to genetic variation. Two Escherichia coli proteins, RuvA and RuvB, promote the formation of heteroduplex DNA by catalysing the branch migration of crossovers, or Holliday junctions, which link recombining chromosomes. We show that RuvA and RuvB can promote branch migration through 1800 bp of heterologous DNA, in a reaction facilitated by the presence of E.coli single-stranded DNA binding (SSB) protein. Reaction intermediates, containing unpaired heteroduplex regions bound by SSB, were directly visualized by electron microscopy. In the absence of SSB, or when SSB was replaced by a single-strand binding protein from bacteriophage T4 (gene 32 protein), only limited heterologous branch migration was observed. These results show that the RuvAB proteins, which are induced as part of the SOS response to DNA damage, allow genetic recombination and the recombinational repair of DNA to occur in the presence of extensive lengths of heterology.
Mots-clé
Adenosine Triphosphatases/antagonists &amp, inhibitors, Adenosine Triphosphatases/metabolism, Bacterial Proteins/metabolism, DNA Helicases/metabolism, DNA, Bacterial/chemistry, DNA, Bacterial/metabolism, DNA, Recombinant, DNA, Single-Stranded, DNA-Binding Proteins/metabolism, Escherichia coli/metabolism, Escherichia coli Proteins, Hela Cells, Humans, Nucleic Acid Heteroduplexes/chemistry, Nucleic Acid Heteroduplexes/metabolism, Substrate Specificity
Pubmed
Web of science
Création de la notice
24/01/2008 10:35
Dernière modification de la notice
20/08/2019 13:09
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