Rad54 protein possesses chromatin-remodeling activity stimulated by the Rad51–ssDNA nucleoprotein filament

Alexeev, Andrei; Mazin, Alexander V.; Kowalczykowski, Stephen C.

doi:10.1038/nsb901

Cited by 220 publications

(179 citation statements)

References 17 publications

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“…As shown in Figure 1B, incubation of the chromatinized template with Rad54 protein rendered it more sensitive to HaeIII, and, consistent with previously published data [12][13][14], the chromatin remodeling reaction was greatly enhanced upon the inclusion of Rad51 (lanes 7 to 9). As expected, Rad51 on its own did not exhibit any chromatin remodeling activity (Fig.…”

Section: Dependence Of Rad51/rad54-mediated Chromatin Remodeling On Psupporting

confidence: 89%

“…As a result of DNA translocation, Rad54 induces dynamic topological changes and transient strand opening in the DNA [9,10]. Like many members of the Swi2/Snf2 protein family, Rad54 remodels chromatin structure, and this chromatin remodeling activity requires ATP hydrolysis [12][13][14]. Moreover, Rad54 utilizes the free energy from ATP hydrolysis to accelerate the DNA strand transfer reaction [15,16] and to process branched DNA structures [16], including the Holliday junction [16], that are expected to be generated during certain HR reactions [17].…”

Section: Introductionmentioning

confidence: 99%

“…Thus, Rad54 plays a major role in regulating the activities of Rad51. Reciprocally, the enzymatic activities of Rad54 -ATP hydrolysis, DNA supercoiling, DNA strand opening, DNA branch migration, and chromatin remodeling -are enhanced by Rad51 [9,[12][13][14]16,35]. In strains deleted for RAD54, ssDNA associated with a site-specific DSB at the MAT locus can synapse with its homologous donor sequence, but DNA strand invasion appears to be impaired [33,36].…”

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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Section: Dependence Of Rad51/rad54-mediated Chromatin Remodeling On Psupporting

confidence: 89%

Section: Introductionmentioning

confidence: 99%

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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“…These models were intuitive and provided important initial concepts. However, all remodeler ATPases are classified as members of the SF2 family of DEAD/H-box helicase/translocases, and a significant advance was the demonstration that remodelers are indeed ATP-dependent DNA translocases 4,5,[35][36][37][38] . This indicated a possible motor force for breaking histone-DNA contacts and moving DNA on the octamer surface.…”

Section: Remodelers Can Translocate Dna From a Fixed Internal Sitementioning

confidence: 99%

Chromatin remodeling: insights and intrigue from single-molecule studies

Cairns

2007

Nat Struct Mol Biol

227

208

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Chromatin remodelers are ATP-hydrolyzing machines specialized to restructure, mobilize or eject nucleosomes, allowing regulated exposure of DNA in chromatin. Recently, remodelers have been analyzed using single-molecule techniques in real time, revealing them to be complex DNA-pumping machines. The results both support and challenge aspects of current models of remodeling, supporting the idea that the remodeler translocates or pumps DNA loops into and around the nucleosome, while also challenging earlier concepts about loop formation, the character of the loop and how it propagates. Several complex behaviors were observed, such as reverse translocation and long translocation bursts of the remodeler, without appreciable DNA twist. This review presents and discusses revised models for nucleosome sliding and ejection that integrate this new information with the earlier biochemical studies.Many processes involving chromosomes are guided by DNA-binding proteins, and the access of these proteins to DNA is regulated by chromatin. Nucleosomes, the primary repeating unit of chromatin, package DNA by wrapping 147 base pairs (bp) around an octamer of histone proteins in ∼1.7 helical turns 1-3 . This packaging provides topological order but occludes one face of the DNA, which slows or prevents the recognition of DNA sequences by DNA-binding proteins. To maintain topological order, and also to allow rapid and regulated access to the DNA, cells have evolved a set of chromatin-remodeling machines that alter nucleosome position, presence and structure.Remodelers can be separated into several families on the basis of their composition and activities: SWI/SNF, ISWI, NURD/Mi-2/CHD and the 'split ATPases' INO80 and SWR1 (which bear an insertion within their ATPase domains). Rad54 may represent an additional family, as it perturbs chromatin in vitro, but it apparently lacks specific nucleosome-interacting domains 4,5 . The participation of remodelers in various chromosomal processes has been the subject of many reviews 6-9 . The present work focuses solely on remodeler mechanisms, and primarily on the function of their conserved catalytic subunit, a superfamily 2 (SF2) ATPdependent DNA translocase. Recently, single-molecule approaches have been used to examine several remodelers, providing many new insights into their behavior. Here I discuss these recent studies, compare them with previous biochemical studies and suggest refinements to existing models to account for some of the observations. Remodelers slide, eject and restructure nucleosomesRemodelers can affect nucleosomes in at least four ways ( Fig. 1): (i) sliding, or moving the histone octamer to a new position, which exposes DNA 10-12 ; (ii) ejection, or completely displacing the octamer to expose DNA [13][14][15][16] ; (iii) removal of H2A-H2B dimers, leaving only the central H3-H4 tetramer, which exposes DNA and destabilizes the nucleosome 17,18 ; and (iv) dimer replacement-for example, exchanging the resident H2A-H2B dimers for dimers NIH Public Access

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“…Helicases alter DNA and RNA structures, remodel chromatin [24, 51, [61][62][63][64][65], and modulate access to the DNA template by transcriptional machinery. RNA polymerases that are involved in the elongation of RNA transcripts have been considered as helicases that unwind the dsDNA to expose the ssDNA strand that serves as the template for RNA synthesis [2].…”

Section: Functions Of Helicasesmentioning

confidence: 99%

Erratum to: Structure and Mechanisms of SF1 DNA Helicases

Raney

Byrd

Aarattuthodiyil

2012

Advances in Experimental Medicine and Biology

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Superfamily I is a large and diverse group of monomeric and dimeric helicases defined by a set of conserved sequence motifs. Members of this class are involved in essential processes in both DNA and RNA metabolism in all organisms. In addition to conserved amino acid sequences, they also share a common structure containing two RecA-like motifs involved in ATP binding and hydrolysis and nucleic acid binding and unwinding. Unwinding is facilitated by a "pin" structure which serves to split the incoming duplex. This activity has been measured using both ensemble and single-molecule conditions. SF1 helicase activity is modulated through interactions with other proteins.

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Rad54 protein possesses chromatin-remodeling activity stimulated by the Rad51–ssDNA nucleoprotein filament

Cited by 220 publications

References 17 publications

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

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

Chromatin remodeling: insights and intrigue from single-molecule studies

Erratum to: Structure and Mechanisms of SF1 DNA Helicases

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