ATP-dependent branch migration of holliday junctions promoted by the RuvA and RuvB proteins of E. coli

Tsaneva, Irina R.; Müller, Berndt; West, Stephen C.

doi:10.1016/0092-8674(92)90638-s

Cited by 242 publications

(180 citation statements)

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“…A tetramer of the RuvA protein recognizes and binds to the junction center (30,31). It recruits the RuvB helicase, which ''pulls'' the junction arms through its ''donut-like'' structure and catalyzes branch migration (32,33). Finally, the RuvC junction resolvase binds as a dimer to the junction-RuvA-RuvB complex on the opposite side of RuvA and cleaves two of the four strands to leave ligatable nicks (34,35).…”

Section: Resultsmentioning

confidence: 99%

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Holliday junction-binding peptides inhibit distinct junction-processing enzymes

Kepple

Boldt

Segall

2005

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

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Holliday junctions (HJ) are the central intermediates in both homologous recombination and site-specific recombination performed by tyrosine recombinases such as the bacteriophage Integrase (Int) protein. Previously, our lab identified peptide inhibitors of Int-mediated recombination that prevent the resolution of HJ intermediates. We now show that two of these inhibitors bind HJ DNA in the square-planar conformation even in the absence of Int protein. The peptides prevent unwinding of branched DNA substrates by the RecG helicase of Escherichia coli and interfere with the resolution of HJ substrates by the RuvABC complex. Our results suggest that these peptides target all proteins that process HJ in the square-planar conformation. These inhibitors should be extremely useful for dissecting homologous recombination and recombination-dependent repair in vitro and in vivo.homologous recombination ͉ recombination-dependent repair ͉ RecG helicase ͉ RuvABC resolvasome ͉ tyrosine recombinase H olliday junctions (HJ), or four-way junctions, are central intermediates in homologous recombination, repair of collapsed replication forks, and reactions performed by the tyrosine recombinase family of site-specific enzymes (1-5). The first two processes are important in all organisms and are involved in the maintenance of chromosome integrity and repair of DNA damage. In the case of diploid organisms, faithful chromosome segregation depends on homologous recombination (6). Sitespecific recombination reactions performed by tyrosine recombinases are also very widespread and control gene expression, regulate plasmid and bacterial chromosome copy number, and mediate lysogeny (3). The presence and disappearance of HJ, their level within cells, and the enzymes that both generate and resolve them are of intense interest. More tools would be extremely useful for both in vitro and in vivo dissection of homologous recombination and repair processes in all organisms.Phage integrase (Int) binds to and mediates strand exchange between pairs of att sites. During recombination, one round of DNA cleavage, strand exchange, and ligation of the top strands of each partner DNA molecule generates a HJ intermediate, which is resolved by a second round of the same catalytic steps (3). These reactions are both rapid and highly reversible, making intermediates very difficult to study.We have identified peptides that inhibit recombination by trapping the protein-bound HJ intermediate and preventing its resolution either to substrates or to products (7-9). The most potent inhibitory peptide, WRWYCR, traps virtually all HJ formed during a reaction and has an IC 50 of 5-20 nM (9). A related peptide, KWWCRW, is very similar to WRWYCR in potency (8). These peptides also inhibit the mechanistically related Cre, XerC and D, and Flp proteins (ref. 9; A.M.S., unpublished results; A. Conway and P. A. Rice, personal communication). Because these proteins share little primary sequence identity, we reasoned that these peptides might interact with free HJ.HJ adopt one...

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Section: Resultsmentioning

confidence: 99%

“…In addition to the RuvABC complex, several subcomplexes also have partial activities, at least in vitro. The RuvAB complex can branch migrate a junction in the absence of RuvC (30,32). A RuvAC or a RuvBC complex can catalyze junction cleavage, albeit less efficiently than the RuvABC complex (13,36,37).…”

Section: Resultsmentioning

confidence: 99%

Holliday junction-binding peptides inhibit distinct junction-processing enzymes

Kepple

Boldt

Segall

2005

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

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“…The concerted actions of RuvA, RuvB and RuvC proteins complete the homologous recombination process by resolving the Holliday junctions into two recombinant duplex DNA molecules West 1997). RuvA and RuvB form a complex that promotes branch migration (Iwasaki et al 1992;Parsons et al 1992;Tsaneva et al 1992). In this reaction, RuvA specifically binds the junction and targets RuvB to it (Iwasaki et al 1992;Parsons et al 1992).…”

Section: Introductionmentioning

confidence: 99%

Mutational analysis on structure–function relationship of a Holliday junction specific endonuclease RuvC

et al. 1998

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“…1D). In practice, a four-stranded reaction must be initiated by a three-stranded pairing reaction catalyzed by a DNA-pairing protein, after which the heteroduplex is extended into duplex regions through the action of the DNA-pairing protein or of an associated DNA helicase/translocase (Das Gupta et al 1981;Kim et al 1992;Tsaneva et al 1992). …”

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confidence: 99%

DNA-Pairing and Annealing Processes in Homologous Recombination and Homology-Directed Repair

Morrical

2015

Cold Spring Harb Perspect Biol

112

127

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The formation of heteroduplex DNA is a central step in the exchange of DNA sequences via homologous recombination, and in the accurate repair of broken chromosomes via homology-directed repair pathways. In cells, heteroduplex DNA largely arises through the activities of recombination proteins that promote DNA-pairing and annealing reactions. Classes of proteins involved in pairing and annealing include RecA-family DNA-pairing proteins, single-stranded DNA (ssDNA)-binding proteins, recombination mediator proteins, annealing proteins, and nucleases. This review explores the properties of these pairing and annealing proteins, and highlights their roles in complex recombination processes including the double Holliday junction (DhJ) formation, synthesis-dependent strand annealing, and singlestrand annealing pathways-DNA transactions that are critical both for genome stability in individual organisms and for the evolution of species.

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ATP-dependent branch migration of holliday junctions promoted by the RuvA and RuvB proteins of E. coli

Cited by 242 publications

References 31 publications

Holliday junction-binding peptides inhibit distinct junction-processing enzymes

Holliday junction-binding peptides inhibit distinct junction-processing enzymes

Mutational analysis on structure–function relationship of a Holliday junction specific endonuclease RuvC

DNA-Pairing and Annealing Processes in Homologous Recombination and Homology-Directed Repair

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