Asf1 Is Required for Viability and Chromatin Assembly during DNA Replication in Vertebrate Cells

Sanematsu, Fumiyuki; Yasuda, Takami; Barman, Hirak Kumar; Fukagawa, Tatsuo; Ono, Tatsuya; Shibahara, Kei-ichi; Nakayama, Tatsuo

doi:10.1074/jbc.m511590200

Cited by 88 publications

(76 citation statements)

References 49 publications

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“…The physiological relevance of our finding that ASF1a binds to both HIRA and CAF-1 p60 through the same domain is reinforced by additional cellular studies recently reported by Sanematsu et al 35 . In this study, the authors reported that an ASF1a(E36A,D37A) mutant, when stably expressed in a conditional ASF1a-knockout chicken DT40 cell line, failed to interact with CAF-1 p60.…”

Section: Discussionsupporting

confidence: 70%

Structure of a human ASF1a–HIRA complex and insights into specificity of histone chaperone complex assembly

Tang

Poustovoitov

Zhao

et al. 2006

Nat Struct Mol Biol

167

245

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Human HIRA, ASF1a, ASF1b and CAF-1 are evolutionally conserved histone chaperones that form multiple functionally distinct chromatin assembly complexes, with roles linked to diverse nuclear process, such as DNA replication and formation of heterochromatin in senescent cells. We report the crystal structure of an ASF1a/HIRA heterodimer and a biochemical dissection of ASF1a's mutually exclusive interactions with HIRA and the p60 subunit of CAF-1. The HIRA B-domain forms an antiparallel β-hairpin that binds perpendicular to the strands of the β-sandwich of ASF1a, via β-sheet, salt-bridge and van der Waals contacts. The N-and C-terminal regions of ASF1a and ASF1b determine the different affinities of these two proteins for HIRA, by contacting regions outside the HIRA B-domain. CAF-1 p60 also employs B-domain-like motifs for binding to ASF1a, thereby competing with HIRA. Together, these studies begin to define the molecular determinants of assembly of functionally diverse macromolecular histone chaperone complexes. KeywordsHistone Deposition; Chromatin Regulation; Histone Chaperones; ASF1; HIRA; CAF-1The basic repeating unit of eukaryotic chromatin is the core nucleosome. Each core nucleosome consists of a histone (H3/H4) 2 heterotetramer, two histone (H2A/H2B) heterodimers and about 147 base pairs of DNA. During chromatin assembly, histone chaperones donate histones to DNA 1 . In human cells, the deposition of the histone H3/H4 complex involves four histone chaperones, Chromatin Assembly Factor 1 (CAF-1), HIstone Regulatory Homolog A (HIRA), and two Anti-Silencing Factor paralogs (ASF1a and ASF1b).CAF-1, an evolutionarily conserved heterotrimeric chaperone comprised of p150, p60 and p48 subunits, mediates DNA synthesis-coupled chromatin assembly in S-phase 1,2 . CAF-1 is also 4 Correspondence should be addressed to R.M. or P.D. A., Ronen Marmorstein, Tel: (215) FAX: (215) marmor@wistar.org, Peter D. Adams, Tel: (215) FAX: (215) 728 3616, Peter.Adams@fccc.edu. 5 Y.T. and M.V.P contributed equally to this work.The coordinates of the ASF1a/HIRA complex structure has been deposited with the Protein Data Bank (PDB) with access code 2I32. COMPETING INTERESTS STATEMENTThe authors declare that they have no competing financial interests. AUTHOR CONTRIBUTIONSY.T. and M.V.P. designed and carried out experiments reported in the manuscript, and prepared manuscript figures and text; K.Z., M.G., A.C. and R.D. carried out preliminary studies that led to experiments reported in the manuscript; P.D.A and R.M. designed and supervised experiments and prepared manuscript text. All authors read and approved the submitted manuscript. NIH Public Access Author ManuscriptNat Struct Mol Biol. Author manuscript; available in PMC 2010 September 6. NIH-PA Author ManuscriptNIH-PA Author Manuscript NIH-PA Author Manuscript required for chromatin assembly coupled to DNA repair 3-8 , formation of specialized chromatin structures, such as transcriptionally silent chromatin at telomeres, rDNA yeast mating loci, and plant gene loci 3,...

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Section: Discussionsupporting

confidence: 70%

Structure of a human ASF1a–HIRA complex and insights into specificity of histone chaperone complex assembly

Tang

Poustovoitov

Zhao

et al. 2006

Nat Struct Mol Biol

167

245

View full text Add to dashboard Cite

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“…In addition to functioning together in vitro, Asf1 and CAF1 are likely to assemble chromatin onto newly-replicated DNA in cells. For example, Asf1 and CAF-1 localize to DNA replication forks [21,22] and their inactivation results in major defects in chromatin assembly of the newly-replicated DNA in cells [23,24]. H2A/H2B deposition following DNA replication is presumably also mediated by histone chaperones, where possible candidates include the NAP1/SET/TAFI [25] and FACT/SPN proteins [26].…”

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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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“…In cellular DNA replication, the Asf1 proteins are critical for managing the flow of histones and the progression of the replication fork via coordinated disassembly and reassembly of nucleosomes. In this capacity, recipient Asf1 proteins are associated with the replicative helicase MCM complex for disassembly and transfer of histone H3/4 ahead of the advancing replication fork to the histone donor Asf1/CAF-1/PCNA complex for reassembly on replicated DNA (21,(29)(30)(31). Asf1 mutations or depletion of the proteins results in defects in replication fork progression (23).…”

mentioning

confidence: 99%

Transcriptional coactivator HCF-1 couples the histone chaperone Asf1b to HSV-1 DNA replication components

Peng

Nogueira

Vogel

et al. 2010

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

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The cellular transcriptional coactivator HCF-1 interacts with numerous transcription factors as well as other coactivators and is a component of multiple chromatin modulation complexes. The protein is essential for the expression of the immediate early genes of both herpes simplex virus (HSV) and varicella zoster virus and functions, in part, by coupling chromatin modification components including the Set1 or MLL1 histone methyltransferases and the histone demethylase LSD1 to promote the installation of positive chromatin marks and the activation of viral immediately early gene transcription. Although studies have investigated the role of HCF-1 in both cellular and viral transcription, little is known about other processes that the protein may be involved in. Here we demonstrate that HCF-1 localizes to sites of HSV replication late in infection. HCF-1 interacts directly and simultaneously with both HSV DNA replication proteins and the cellular histone chaperone Asf1b, a protein that regulates the progression of cellular DNA replication forks via chromatin reorganization. Asf1b localizes with HCF-1 in viral replication foci and depletion of Asf1b results in significantly reduced viral DNA accumulation. The results support a model in which the transcriptional coactivator HCF-1 is a component of the HSV DNA replication assembly and promotes viral DNA replication by coupling Asf1b to DNA replication components. This coupling provides a novel function for HCF-1 and insights into the mechanisms of modulating chromatin during DNA replication.

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Asf1 Is Required for Viability and Chromatin Assembly during DNA Replication in Vertebrate Cells

Cited by 88 publications

References 49 publications

Structure of a human ASF1a–HIRA complex and insights into specificity of histone chaperone complex assembly

Structure of a human ASF1a–HIRA complex and insights into specificity of histone chaperone complex assembly

Chromatin disassembly and reassembly during DNA repair

Transcriptional coactivator HCF-1 couples the histone chaperone Asf1b to HSV-1 DNA replication components

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