HIRA Is Critical for a Nucleosome Assembly Pathway Independent of DNA Synthesis

Ray-Gallet, Dominique; Quivy, Jean‐Pierre; Scamps, Christine; Martini, Emmanuelle; Lipinski, Marc; Almouzni, Geneviève

doi:10.1016/s1097-2765(02)00526-9

Cited by 378 publications

(302 citation statements)

References 57 publications

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“…Mouse ES cells lacking HIRA have a larger pool of loosely bound histones than wild type cells, consistent with a role for HIRA in generation of compact, nucleosome-dense, transcriptionally silent heterochromatin (78). In vitro, HIRA has been shown to act as a histone chaperone, preferentially depositing the histone variant histone H3.3 into nucleosomes, compared to canonical histone H3.1 (49,72,100,102,125). Consistent with their partially overlapping functions, Asf1 and Hir proteins physically interact and in yeast this interaction is necessary for telomeric silencing (32,49,116).…”

Section: Chromosome Condensation Is Driven By Histone Chaperones Hiramentioning

confidence: 57%

Remodeling of chromatin structure in senescent cells and its potential impact on tumor suppression and aging

Adams

2007

Gene

162

135

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Cellular senescence is an important tumor suppression process, and a possible contributor to tissue aging. Senescence is accompanied extensive changes in chromatin structure. In particular, many senescent cells accumulate specialized domains of facultative heterochromatin, called Senescence Associated Heterochromatin Foci (SAHF), which are thought to repress expression of proliferationpromoting genes, thereby contributing to senescence-associated proliferation arrest. This article reviews our current understanding of the structure, assembly and function of these SAHF at a cellular level. The possible contribution of SAHF to tumor suppression and tissue aging is also critically discussed.

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Section: Chromosome Condensation Is Driven By Histone Chaperones Hiramentioning

confidence: 57%

Remodeling of chromatin structure in senescent cells and its potential impact on tumor suppression and aging

Adams

2007

Gene

162

135

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“…CAF-1, which is composed of three subunits p150, p60 and RbAp48, represents the prototype of a chaperone that promotes nucleosome assembly in a DSC pathway during replication and UV-damage repair [58,59]. In contrast, HIRA was described as a chaperone involved in the DSI nucleosome assembly pathway in vitro using the X. laevis egg extract system and shows a critical role in H3.3 deposition [57,60]. The genome-wide enrichment of H3.3 at promoters and in the body of active genes is affected in HIRA knockout ES cells, suggesting a critical requirement for HIRA in H3.3 deposition at these specific regions (Figure 3) [24].…”

Section: Hira Complexmentioning

confidence: 99%

The double face of the histone variant H3.3

Szenker¹,

Ray-Gallet²,

Almouzni³

2011

Cell Res

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338

308

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Histone proteins wrap DNA to form nucleosome particles that compact eukaryotic genomes while still allowing access for cellular processes such as transcription, replication and DNA repair. Histones exist as different variants that have evolved crucial roles in specialized functions in addition to their fundamental role in packaging DNA. H3.3 -a conserved histone variant that is structurally very close to the canonical histone H3 -has been associated with active transcription. Furthermore, its role in histone replacement at active genes and promoters is highly conserved and has been proposed to participate in the epigenetic transmission of active chromatin states. Unexpectedly, recent data have revealed accumulation of this specific variant at silent loci in pericentric heterochromatin and telomeres, raising questions concerning the actual function of H3.3. In this review, we describe the known properties of H3.3 and the current view concerning its incorporation modes involving particular histone chaperones. Finally, we discuss the functional significance of the use of this H3 variant, in particular during germline formation and early development in different species.

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“…Inhibition of CAF-1 blocks S-phase progression in human cells, suggesting that replication-coupled nucleosome assembly is essential (Hoek and Stillman 2003;Ye et al 2003). Replication-independent histone deposition is carried out by a number of histone chaperones including the Hir proteins (Ray-Gallet et al 2002;Tagami et al 2004; for review, see Franco and Kaufman 2004).…”

mentioning

confidence: 99%

Histone deposition protein Asf1 maintains DNA replisome integrity and interacts with replication factor C

Franco¹,

Lam²,

Burgers³

et al. 2005

Genes Dev.

128

125

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Chromatin assembly and DNA replication are temporally coupled, and DNA replication in the absence of histone synthesis causes inviability. Here we demonstrate that chromatin assembly factor Asf1 also affects DNA replication. In budding yeast cells lacking Asf1, the amounts of several DNA replication proteins, including replication factor C (RFC), proliferating cell nuclear antigen (PCNA), and DNA polymerase (Pol ), are reduced at stalled replication forks. In contrast, DNA polymerase ␣ (Pol ␣) accumulates to higher than normal levels at stalled forks in asf1⌬ cells. Using purified, recombinant proteins, we demonstrate that RFC directly binds Asf1 and can recruit Asf1 to DNA molecules in vitro. We conclude that histone chaperone protein Asf1 maintains a subset of replication elongation factors at stalled replication forks and directly interacts with the replication machinery.[Keywords: Chromatin assembly; histone deposition; DNA replication; genome stability] Supplemental material is available at http://www.genesdev.org. In eukaryotes, DNA is assembled into a nucleoprotein complex called chromatin. The fundamental repeating unit of chromatin is the nucleosome, which consists of 146 bp of DNA wrapped around an octamer of core histone proteins, comprised of two H2A/H2B dimers flanking an inner (H3/H4) 2 tetramer. In vivo, histone deposition can occur by DNA replication-coupled or replication-independent mechanisms (for review, see Franco and Kaufman 2004). In either case, histone deposition is mediated by specialized assembly proteins. The best characterized replication-coupled chromatin assembly factor is chromatin assembly factor-1 (CAF-1), an evolutionarily conserved protein complex that binds histone H3 and H4 and delivers them to replicating DNA through an interaction with proliferating cell nuclear antigen (PCNA), the DNA polymerase processivity protein (for review, see Asf1, another evolutionarily conserved histone chaperone, functions during both replication-coupled and replication-independent chromatin assembly. Asf1 bound to histones H3/H4 stimulates histone deposition by CAF-1 in vitro (Tyler et al. 1999;Sharp et al. 2001), and Asf1 physically interacts with the p60/Cac2 subunit of CAF-1 (Tyler et al. 2001;Krawitz et al. 2002;Mello et al. 2002). In yeast, Asf1 and the Hir proteins directly interact and function together to promote heterochromatic gene silencing (Kaufman et al. 1998;Sharp et al. 2001;Sutton et al. 2001;Krawitz et al. 2002). Consistent with a role in multiple deposition pathways, Asf1 copurifies with both CAF-1 and Hir protein complexes in human cell extracts (Tagami et al. 2004).Asf1 also contributes to genome stability during S phase in a manner distinct from both CAF-1 and the Hir proteins. Unlike yeast cells lacking CAF-1 or Hir proteins, cells lacking Asf1 are sensitive to the DNA synthesis inhibitor hydroxyurea (HU) and the DNA topoisomerase I inhibitor camptothecin (CPT), and display synthetic genetic interactions with DNA synthesis genes including the initiation/elongation factor C...

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HIRA Is Critical for a Nucleosome Assembly Pathway Independent of DNA Synthesis

Cited by 378 publications

References 57 publications

Remodeling of chromatin structure in senescent cells and its potential impact on tumor suppression and aging

Remodeling of chromatin structure in senescent cells and its potential impact on tumor suppression and aging

The double face of the histone variant H3.3

Histone deposition protein Asf1 maintains DNA replisome integrity and interacts with replication factor C

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