ATP-Driven Exchange of Histone H2AZ Variant Catalyzed by SWR1 Chromatin Remodeling Complex

Mizuguchi, Gaku; Shen, Xuetong; Landry, Joe; Wu, Wei; Sen, Subhojit; Wu, Carl

doi:10.1126/science.1090701

Cited by 1,186 publications

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“…Perhaps the most specialized function of remodelers involves histone-variant exchange. Only SWR1 efficiently replaces H2A-H2B dimers with Htz1-H2B dimers in vitro 19 , and new in vivo evidence supports a role for the INO80 remodeler in the reverse reaction, which may be important for recovery from DNA repair 26 .…”

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confidence: 89%

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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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confidence: 89%

“…19 ). In yeast, Htz1 nucleosomes are highly enriched at gene promoters 20,21 and help promote gene activation and efficient DNA repair.…”

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confidence: 99%

Chromatin remodeling: insights and intrigue from single-molecule studies

Cairns

2007

Nat Struct Mol Biol

227

208

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“…Deletion of Saccharomyces cerevisiae SWR1 causes sensitivity to MMS and moderate sensitivity to UV [47]. Interestingly, SWR1 also mediates the removal of histone H2A from chromatin and its replacement by the histone variant H2AZ, although it is not known if this occurs during DNA repair [47].…”

Section: Asf1mentioning

confidence: 99%

“…Interestingly, SWR1 also mediates the removal of histone H2A from chromatin and its replacement by the histone variant H2AZ, although it is not known if this occurs during DNA repair [47].…”

Section: Asf1mentioning

confidence: 99%

Chromatin disassembly and reassembly during DNA repair

Linger

Tyler

2007

Mutation Research/Fundamental and Molecular Mechanisms of Mutag

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Current research is demonstrating that the packaging of the eukaryotic genome together with histone proteins into chromatin is playing a fundamental role in DNA repair and the maintenance of genomic integrity. As is well established to be the case for transcription, the chromatin structure dynamically changes during DNA repair. Recent studies indicate that the complete removal of histones from DNA and their subsequent reassembly onto DNA accompanies DNA repair. This review will present evidence indicating that chromatin disassembly and reassembly occur during DNA repair and that these are critical processes for cell survival after DNA repair. Concomitantly, candidate proteins utilized for these processes will be highlighted.

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“…The CHD subfamily is differentiated by an ATPase that contains a chromodomain and PHD fingers [6,7]. The INO80 subfamily includes the INO80 remodeling complex (INO80.com) and the SWR1 remodeling complex (SWR1.com) which are characterized by split ATPase domains (Ino80 and Swr1 respectively, see Figure 1) and the presence of two RuvB-like proteins, Rvb1 and Rvb2 [8,9]. The purpose of this review is to integrate and discuss the current knowledge of the biochemical composition and cellular functions of these two recently characterized ATP-dependent chromatin remodeling complexes.…”

Section: Introductionmentioning

confidence: 99%

INO80 subfamily of chromatin remodeling complexes

Bao

Shen

2007

Mutation Research/Fundamental and Molecular Mechanisms of Mutag

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110

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ATP-dependent chromatin remodeling complexes contain ATPases of the Swi/Snf superfamily and alter DNA accessibility of chromatin in an ATP-dependent manner. Recently characterized INO80 and SWR1 complexes belong to a subfamily of these chromatin remodelers and are characterized by a split ATPase domain in the core ATPase subunit and the presence of Rvb proteins. INO80 and SWR1 complexes are evolutionarily conserved from yeast to human and have been implicated in transcription regulation, as well as DNA repair. The individual components, assembly patterns, and molecular mechanisms of the INO80 class of chromatin remodeling complexes are discussed in this review.

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ATP-Driven Exchange of Histone H2AZ Variant Catalyzed by SWR1 Chromatin Remodeling Complex

Cited by 1,186 publications

References 36 publications

Chromatin remodeling: insights and intrigue from single-molecule studies

Chromatin remodeling: insights and intrigue from single-molecule studies

Chromatin disassembly and reassembly during DNA repair

INO80 subfamily of chromatin remodeling complexes

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