Rad51 Recombinase and Recombination Mediators

Sung, Patrick; Krejčí, Lumír; Komen, Stephen Van; Sehorn, Michael G.

doi:10.1074/jbc.r300027200

Cited by 383 publications

(357 citation statements)

References 64 publications

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“…However, when an excess of RPA is added to ssDNA prior to RAD51, strand exchange is inhibited. This inhibition is overcome by recombination mediators, like RAD52, another type of ssDNA binding protein that stimulates RAD51 strand-exchange in the postinvasion steps (Sung et al, 2003). In addition, colocalization of RPA, RAD51, and RAD52 further confirms that RPA participates in these processes in budding yeast (McIlwraith et al, 2000).…”

Section: Introductionmentioning

confidence: 65%

Replication Protein A2c Coupled with Replication Protein A1c Regulates Crossover Formation during Meiosis in Rice

Chang

Xin

et al. 2013

The Plant Cell

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Replication protein A (RPA) is a conserved heterotrimeric protein complex comprising RPA1, RPA2, and RPA3 subunits involved in multiple DNA metabolism pathways attributable to its single-stranded DNA binding property. Unlike other species possessing a single RPA2 gene, rice (Oryza sativa) possesses three RPA2 paralogs, but their functions remain unclear. In this study, we identified RPA2c, a rice gene preferentially expressed during meiosis. A T-DNA insertional mutant (rpa2c) exhibited reduced bivalent formation, leading to chromosome nondisjunction. In rpa2c, chiasma frequency is reduced by ;78% compared with the wild type and is accompanied by loss of the obligate chiasma. The residual ;22% chiasmata fit a Poisson distribution, suggesting loss of crossover control. RPA2c colocalized with the meiotic cohesion subunit REC8 and the axis-associated protein PAIR2. Localization of REC8 was necessary for loading of RPA2c to the chromosomes. In addition, RPA2c partially colocalized with MER3 during late leptotene, thus indicating that RPA2c is required for class I crossover formation at a late stage of homologous recombination. Furthermore, we identified RPA1c, an RPA1 subunit with nearly overlapping distribution to RPA2c, required for ;79% of chiasmata formation. Our results demonstrate that an RPA complex comprising RPA2c and RPA1c is required to promote meiotic crossovers in rice.

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Section: Introductionmentioning

confidence: 65%

Replication Protein A2c Coupled with Replication Protein A1c Regulates Crossover Formation during Meiosis in Rice

Chang

Xin

et al. 2013

The Plant Cell

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“…Although many of the key proteins involved in HRR have been identified (reviewed in Paques and Haber, 1999;Sung et al, 2003;West, 2003;Krogh and Symington, 2004), in some cases their precise function(s) remains to be identified. Moreover, the mechanisms for suppression of inappropriate HRR in S-phase are only poorly defined.…”

Section: Introductionmentioning

confidence: 99%

Shu Proteins Promote the Formation of Homologous Recombination Intermediates That Are Processed by Sgs1-Rmi1-Top3

Mankouri

Ngo

Hickson

2007

MBoC

125

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CSM2, PSY3, SHU1, and SHU2 (collectively referred to as the SHU genes) were identified in Saccharomyces cerevisiae as four genes in the same epistasis group that suppress various sgs1 and top3 mutant phenotypes when mutated. Although the SHU genes have been implicated in homologous recombination repair (HRR), their precise role(s) within this pathway remains poorly understood. Here, we have identified a specific role for the Shu proteins in a Rad51/Rad54-dependent HRR pathway(s) to repair MMS-induced lesions during S-phase. We show that, although mutation of RAD51 or RAD54 prevented the formation of MMS-induced HRR intermediates (X-molecules) arising during replication in sgs1 cells, mutation of SHU genes attenuated the level of these structures. Similar findings were also observed in shu1 cells in which Rmi1 or Top3 function was impaired. We propose a model in which the Shu proteins act in HRR to promote the formation of HRR intermediates that are processed by the Sgs1-Rmi1-Top3 complex. INTRODUCTIONHomologous recombination repair (HRR) is a well-conserved cellular process for the repair of single-strand DNA (ssDNA) gaps and double-strand DNA breaks (DSBs) that can arise during DNA synthesis or as a result of replication fork stalling during S-phase. Although many of the key proteins involved in HRR have been identified (reviewed in Paques and Haber, 1999;Sung et al., 2003;West, 2003;Krogh and Symington, 2004), in some cases their precise function(s) remains to be identified. Moreover, the mechanisms for suppression of inappropriate HRR in S-phase are only poorly defined. It is likely that HRR must be carefully regulated and/or executed in dividing cells, as inappropriate or excessive HR can lead to genome rearrangements and cancer in mammals. This is exemplified by the cancer-predisposition disorder, Bloom's syndrome, which is caused by mutation in the human BLM gene (reviewed in German, 1993). Because the BLM protein, in conjunction with its associated proteins, hTOPOIII␣ and hRMI1 (Johnson et al., 2000;Wu et al., 2000;Yin et al., 2005), can catalyze dissolution of HRR intermediates in vitro Plank et al., 2006;Raynard et al., 2006;Wu et al., 2006), it is likely that unprocessed and/or aberrantly processed HRR intermediates at least partly contribute to the cellular defects in Bloom's syndrome. Indeed, Bloom's syndrome cells classically demonstrate elevated levels of sister chromatid exchanges, mitotic recombination, and genome instability. Mutation of the BLM, hTOPOIII␣, or hRMI1 homologues in Saccharomyces cerevisiae (SGS1, TOP3, or RMI1, respectively) similarly causes sensitivity to genotoxic agents, hyper-recombination, and synthetic lethality with mutations in other genes also implicated in HRR (e.g., MUS81 and SRS2; Gangloff et al., 1994;Watt et al., 1996;Gangloff et al., 2000;Mullen et al., 2001;Fabre et al., 2002;Chang et al., 2005;Mullen et al., 2005). Furthermore, unresolved HRR intermediates have been directly visualized by two-dimensional (2D) gel electrophoresis in cells lacking Sgs1 or in cells w...

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“…The ability of Rad54 to promote Rad51-dependent D-loop formation has been well documented [20]. More recent studies that utilized highly purified S. cerevisiae and D. melanogaster protein factors have shown that Rad54 enables Rad51 to make D-loop with a chromatinized DNA template as well [12,14].…”

Section: Salt Sensitivity Of D-loop Formation By Rad51 and Rad54 δ129mentioning

confidence: 99%

“…D-loop formation is catalyzed by a recombinase enzyme, either Rad51 or Dmc1 [18], in a reaction termed homologous DNA pairing [17,19,20]. Like their prokaryotic counterparts E. coli RecA and T4 UvsX, Rad51 and Dmc1 form a filamentous structure, referred to as the presynaptic filament, on ssDNA [18,19].…”

Section: Introductionmentioning

confidence: 99%

“…Assembly of the presynaptic filament requires ATP binding by the recombinase protein [19,20], and ATP hydrolysis by the DNA-bound recombinase promotes the turnover of the presynaptic filament [21][22][23][24]. All the subsequent biochemical steps, including the capture of the duplex DNA partner and the search for homology in the engaged ssDNA and dsDNA molecules, that lead to D-loop formation occur within the confines of the presynaptic filament [17,19,20]. Thus, the presynaptic filament represents the key catalytic recombinase-DNA complex critical for the successful initiation and completion of the HR reaction.…”

Section: Introductionmentioning

confidence: 99%

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Synergistic action of the Saccharomyces cerevisiae homologous recombination factors Rad54 and Rad51 in chromatin remodeling

et al. 2007

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Rad54, a member of the Swi2/Snf2 protein family, works in concert with the RecA-like recombinase Rad51 during the early and late stages of homologous recombination. Rad51 markedly enhances the activities of Rad54, including the induction of topological changes in DNA and the remodeling of chromatin structure. Reciprocally, Rad54 promotes Rad51-mediated DNA strand invasion with either naked or chromatinized DNA. Here, using various Saccharomyces cerevisiae rad51 and rad54 mutant proteins, mechanistic aspects of Rad54/Rad51-mediated chromatin remodeling are defined. Disruption of the Rad51-Rad54 complex leads to a marked attenuation of chromatin remodeling activity. Moreover, we present evidence that assembly of the Rad51 presynaptic filament represents an obligatory step in the enhancement of the chromatin remodeling reaction. Interestingly, we find a specific interaction of the N-terminal tail of histone H3 with Rad54 and show that the H3 tail interaction domain resides within the amino terminus of Rad54. These results suggest that Rad54-mediated chromatin remodeling coincides with DNA homology search by the Rad51 presynaptic filament and that this process is facilitated by an interaction of Rad54 with histone H3.

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Rad51 Recombinase and Recombination Mediators

Cited by 383 publications

References 64 publications

Replication Protein A2c Coupled with Replication Protein A1c Regulates Crossover Formation during Meiosis in Rice

Replication Protein A2c Coupled with Replication Protein A1c Regulates Crossover Formation during Meiosis in Rice

Shu Proteins Promote the Formation of Homologous Recombination Intermediates That Are Processed by Sgs1-Rmi1-Top3

Synergistic action of the Saccharomyces cerevisiae homologous recombination factors Rad54 and Rad51 in chromatin remodeling

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