Coordinated actions of RuvABC in Holliday junction processing 1 1Edited by J. Karn

Zerbib, Didier; Mézard, Christine; George, Helen; West, Stephen C.

doi:10.1006/jmbi.1998.1959

Cited by 67 publications

(42 citation statements)

References 46 publications

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“…RuvB can stimulate the binding to and resolution of a HJ by RuvC, and RuvC can stimulate RuvBcatalyzed branch migration in the absence of RuvA (63). RuvAB also clearly stimulated RuvC-catalyzed HJ resolution over a 310-bp homologous region in a fashion that was dependent on the DNA helicase activity of RuvB (64).…”

Section: Discussionmentioning

confidence: 93%

Regression of Replication Forks Stalled by Leading-strand Template Damage

Gupta

Yeeles

Marians

2014

Journal of Biological Chemistry

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Section: Discussionmentioning

confidence: 93%

Regression of Replication Forks Stalled by Leading-strand Template Damage

Gupta

Yeeles

Marians

2014

Journal of Biological Chemistry

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“…On the other hand, the RuvC dimer was found to more efficiently resolve the junction DNA in the presence of both RuvA and RuvB, implying the formation of a higher order complex, termed the RuvABC resolvasome (7,8,30). However, the Holliday junction covered on both sides by RuvA, as in form II, could not be cleaved by RuvC resolvase.…”

Section: Discussionmentioning

confidence: 99%

Crystal structure of the Holliday junction DNA in complex with a single RuvA tetramer

Ariyoshi

Nishino

Iwasaki

et al. 2000

Proc. Natl. Acad. Sci. U.S.A.

123

146

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In the major pathway of homologous DNA recombination in prokaryotic cells, the Holliday junction intermediate is processed through its association with RuvA, RuvB, and RuvC proteins. Specific binding of the RuvA tetramer to the Holliday junction is required for the RuvB motor protein to be loaded onto the junction DNA, and the RuvAB complex drives the ATP-dependent branch migration. We solved the crystal structure of the Holliday junction bound to a single Escherichia coli RuvA tetramer at 3.1-Å resolution. In this complex, one side of DNA is accessible for cleavage by RuvC resolvase at the junction center. The refined junction DNA structure revealed an open concave architecture with a four-fold symmetry. Each arm, with B-form DNA, in the Holliday junction is predominantly recognized in the minor groove through hydrogen bonds with two repeated helix-hairpin-helix motifs of each RuvA subunit. The local conformation near the crossover point, where two base pairs are disrupted, suggests a possible scheme for successive base pair rearrangements, which may account for smooth Holliday junction movement without segmental unwinding.

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“…There is an intriguing parallel with Escherichia coli RuvC resolvase. Zerbib et al (33) showed that stimulation of RuvC by the RuvAB branch migration complex shows dependence on ATP. Because ATP hydrolysis is essential for branch migration activity of RuvAB, they suggested that the process of branch migration is important for RuvC stimulation.…”

Section: Discussionmentioning

confidence: 99%

Human Rad54 protein stimulates human Mus81–Eme1 endonuclease

Mazina

Mazin

2008

Proc. Natl. Acad. Sci. U.S.A.

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Rad54, a key protein of homologous recombination, physically interacts with a DNA structure-specific endonuclease, Mus81-Eme1. Genetic data indicate that Mus81-Eme1 and Rad54 might function together in the repair of damaged DNA. In vitro, Rad54 promotes branch migration of Holliday junctions, whereas the Mus81-Eme1 complex resolves DNA junctions by endonucleolytic cleavage. Here, we show that human Rad54 stimulates Mus81-Eme1 endonuclease activity on various Holliday junction-like intermediates. This stimulation is the product of specific interactions between the human Rad54 (hRad54) and Mus81 proteins, considering that Saccharomyces cerevisiae Rad54 protein does not stimulate human Mus81-Eme1 endonuclease activity. Stimulation of Mus81-Eme1 cleavage activity depends on formation of specific Rad54 complexes on DNA substrates occurring in the presence of ATP and, to a smaller extent, of other nucleotide cofactors. Thus, our results demonstrate a functional link between the branch migration activity of hRad54 and the structurespecific endonuclease activity of hMus81-Eme1, suggesting that the Rad54 and Mus81-Eme1 proteins may cooperate in the processing of Holliday junction-like intermediates during homologous recombination or DNA repair.branch migration ͉ Holliday junction resolution ͉ homologous recombination H omologous recombination (HR) is responsible for the repair of DNA double-stranded breaks (DSB) and faithful chromosome segregation during meiosis (1). The Holliday junction (HJ) is a central intermediate of HR (2). HJs are thought to form during meiotic recombination, DSB repair, and repair of collapsed replication forks (3, 4). At late stages of HR or DNA repair, HJs, which constitute a physical link between DNA molecules, must be resolved to allow chromosome separation. Enzymes that cleave HJs, called HJ resolvases, are structure-specific endonucleases that introduce coordinated single-strand cuts across the junction (5). Several HJ resolvases from bacteriophages, eubacteria, archaea, eukaryotic viruses, and mitochondria have been identified, isolated, and characterized (5). However, the identity of eukaryotic nuclear HJ resolvases is still elusive.A role for Mus81 in HJ resolution was first proposed in studies on Schizosaccharomyces pombe, where Mus81 was identified as a critical factor for the production of viable spores, survival under conditions that lead to stalling of replication fork progression, and viability in the absence of RecQ helicase, Rqh1 (6). All of the defects in S. pombe mus81 mutants were rescued by expression of RusA, a bacteriophage resolvase that is highly specific for HJs (7). Mus81 protein is widely conserved among eukaryotes, including Saccharomyces cerevisiae (8), S. pombe (6), Arabidopsis thaliana (9), mice (10, 11), and humans (12). Mus81 is related to the XPF family of structure-specific endonucleases, which share a highly conserved motif (V/IERKX 3 D) that constitutes an integral part of the endonuclease catalytic site. Mus81 functions as a heterodimer with a noncatalytic p...

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Coordinated actions of RuvABC in Holliday junction processing 1 1Edited by J. Karn

Cited by 67 publications

References 46 publications

Regression of Replication Forks Stalled by Leading-strand Template Damage

Regression of Replication Forks Stalled by Leading-strand Template Damage

Crystal structure of the Holliday junction DNA in complex with a single RuvA tetramer

Human Rad54 protein stimulates human Mus81–Eme1 endonuclease

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