Multiple Links between the NuA4 Histone Acetyltransferase Complex and Epigenetic Control of Transcription

Galarneau, Luc; Nourani, Amine; Boudreault, Alexandre A.; Zhang, Yan; Héliot, Laurent; Allard, Stéphane; Savard, Julie; Lane, William S.; Stillman, David J.; Côté, Jacques

doi:10.1016/s1097-2765(00)80258-0

Cited by 248 publications

(261 citation statements)

References 54 publications

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“…By both chromatin immunoprecipitation and fluorescence localization studies, Esa1p has been defined for its general nuclear roles and distribution (Galarneau et al, 2000;Reid et al, 2000;Vogelauer et al, 2000;Huh et al, 2003). Viewed collectively, the previously observed defects in nucleolar structure , in addition to the rDNA silencing, recombination and PFGE analyses reported here all suggested that ESA1 also contributes to normal nucleolar structure and function.…”

Section: Altered Localization Of Two Nucleolar Proteins In Esa1 Mutantssupporting

confidence: 58%

“…Because Esa1p is an essential histone acetyltransferase with connections to transcriptional activation (Allard et al, 1999;Galarneau et al, 2000;Reid et al, 2000;Eisen et al, 2001), it might be expected that the esa1 temperature-sensitive mutants that have total decreases in histone H4 acetylation would have collateral increases in transcriptional silencing.…”

Section: Esa1 Mutants Are Defective In Transcriptional Silencing At Tmentioning

confidence: 99%

“…Analysis of conditional esa1 mutants reveals that loss of activity results in changes in nuclear substructure and overall decreases in genomic H4 acetylation . Biochemical studies demonstrate that Esa1p is the catalytic subunit of the NuA4 complex that includes other essential subunits such as Tra1p and Act3p and other key subunits with connections to growth control and epigenetic elements of transcriptional activation (Allard et al, 1999;Galarneau et al, 2000). Indeed, a number of distinct transcriptional targets have been identified for Esa1p, along with genome-wide validation of its role as a global H4 HAT (Galarneau et al, 2000;Reid et al, 2000;Vogelauer et al, 2000;Nourani et al, 2001).…”

Section: Expanded Roles For An Essential Myst Family Hatmentioning

confidence: 99%

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Distinct Roles for the Essential MYST Family HAT Esa1p in Transcriptional Silencing

Clarke

Samal

Pillus

2006

MBoC

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Among acetyltransferases, the MYST family enzyme Esa1p is distinguished for its essential function and contribution to transcriptional activation and DNA double-stranded break repair. Here we report that Esa1p also plays a key role in silencing RNA polymerase II (Pol II)-transcribed genes at telomeres and within the ribosomal DNA (rDNA) of the nucleolus. These effects are mediated through Esa1p's HAT activity and correlate with changes within the nucleolus. Esa1p is enriched within the rDNA, as is the NAD-dependent protein deacetylase Sir2p, and the acetylation levels of key Esa1p histone targets are reduced in the rDNA in esa1 mutants. Although mutants of both ESA1 and SIR2 have enhanced rates of rDNA recombination, esa1 effects are more modest yet result in distinct structural changes of rDNA chromatin. Surprisingly, increased expression of ESA1 can bypass the requirement for Sir2p in rDNA silencing, suggesting that these two enzymes with seemingly opposing activities both contribute to achieve optimal nucleolar chromatin structure and function. INTRODUCTIONHistone modifications such as phosphorylation, methylation, acetylation, and deacetylation provide a mechanism by which chromatin structure is modulated to affect gene expression both positively and negatively (for reviews see Strahl and Allis, 2000;Iizuka and Smith, 2003;Kurdistani and Grunstein, 2003). The acetylation of lysine residues on histone N-terminal tails is classically linked to increases in gene expression and more directly to roles in transcriptional activation. By contrast, deacetylation of histones is most frequently correlated with transcriptionally silent chromatin. As more is learned about the enzymes catalyzing these modifications, the histone acetyltransferases (HATs) and histone deacetylases (HDACs), simple functional distinctions between acetylation and deacetylation of histones do not hold (Iizuka and Smith, 2003). For example, in several organisms, mutations in RPD3, a gene encoding a deacetylase, lead to increases in silencing rather than the expected decreases (DeRubertis et al., 1996;Rundlett et al., 1996). This brings forward the possibility that histone acetylation may play an important part in both silent and active chromatin. In addition, coactivator proteins, such as the histone acetyltransferases p300 and CBP and nuclear hormone receptors, appear to have roles in transcriptional repression through acetylation and association with particular binding partners (for examples, see Chen and Li, 1998;Waltzer and Bienz, 1998;Baluchamy et al., 2003;Girdwood et al., 2003;Rajabi et al., 2005). Thus, understanding of multiple roles for acetylation in controlling gene expression is expanding.In Saccharomyces cerevisiae, there are three regions of the genome controlled by chromatin-mediated transcriptional silencing: telomeres, the silent mating-type loci HMR and HML, and the rDNA array. Many factors are important for transcriptional silencing at subsets of these loci including the four core histones, the repressor activator protein Rap1...

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Section: Altered Localization Of Two Nucleolar Proteins In Esa1 Mutantssupporting

confidence: 58%

Section: Esa1 Mutants Are Defective In Transcriptional Silencing At Tmentioning

confidence: 99%

Section: Expanded Roles For An Essential Myst Family Hatmentioning

confidence: 99%

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Distinct Roles for the Essential MYST Family HAT Esa1p in Transcriptional Silencing

Clarke

Samal

Pillus

2006

MBoC

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“…The recruitment of SAGA leads to acetylation of promoter-proximal H3, whereas recruitment of NuA4 results in a broader domain of H4 acetylation (>3 kbp) (Vignali et al, 2000). This hyperacetylation of histones was linked to transcription activation (Nourani et al, 2001) and NuA4-dependent acetylation of histone H4 was shown to affect transcription of specific genes such as His4, Lys2 (Galarneau et al, 2000), ribosomal proteins and heat-shock proteins (Reid et al, 2000). Arabi et al (2005) have shown that TRRAP is recruited by c-Myc to the promoters of Pol I transcribed genes.…”

Section: Transcriptionmentioning

confidence: 99%

Orchestration of chromatin-based processes: mind the TRRAP

et al. 2007

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Chromatin modifications at core histones including acetylation, methylation, phosphorylation and ubiquitination play an important role in diverse biological processes. Acetylation of specific lysine residues within the N terminus tails of core histones is arguably the most studied histone modification; however, its precise roles in different cellular processes and how it is disrupted in human diseases remain poorly understood. In the last decade, a number of histone acetyltransferases (HATs) enzymes responsible for histone acetylation, has been identified and functional studies have begun to unravel their biological functions. The activity of many HATs is dependent on HAT complexes, the multiprotein assemblies that contain one HAT catalytic subunit, adapter proteins, several other molecules of unknown function and a large protein called TRansformation/tRanscription domain-Associated Protein (TRRAP). As a common component of many HAT complexes, TRRAP appears to be responsible for the recruitment of these complexes to chromatin during transcription, replication and DNA repair. Recent studies have shed new light on the role of TRRAP in HAT complexes as well as mechanisms by which it mediates diverse cellular processes. Thus, TRRAP appears to be responsible for a concerted and context-dependent recruitment of HATs and coordination of distinct chromatin-based processes, suggesting that its deregulation may contribute to diseases. In this review, we summarize recent developments in our understanding of the function of TRRAP and TRRAP-containing HAT complexes in normal cellular processes and speculate on the mechanism underlying abnormal events that may lead to human diseases such as cancer.

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“…Interestingly, all subunits of this actin/Arp sub-complex, including the ΔN domain of the Ino80 ATPase are evolutionarily conserved, suggesting that this sub-complex represents a unique and evolutionarily conserved module used throughout the yeast INO80 complex and orthologous INO80 complexes in higher organisms. Since actin and Arp4 are consistently present in several chromatin modifying complexes, such as INO80, SWR1 and NuA4 [8,9,28], and the loss of Arp8 in the INO80 complex results in the loss of actin and Arp4 [10], it can be argued that actin and Arp4 form a dimer and may represent a evolutionarily conserved and basic module involving nuclear actin. This actin/Arp4 module could be used repeatedly in combination with other Arps and proteins in chromatin modifying complexes.…”

Section: Introductionmentioning

confidence: 99%

INO80 subfamily of chromatin remodeling complexes

Bao

Shen

2007

Mutation Research/Fundamental and Molecular Mechanisms of Mutag

106

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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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Multiple Links between the NuA4 Histone Acetyltransferase Complex and Epigenetic Control of Transcription

Cited by 248 publications

References 54 publications

Distinct Roles for the Essential MYST Family HAT Esa1p in Transcriptional Silencing

Distinct Roles for the Essential MYST Family HAT Esa1p in Transcriptional Silencing

Orchestration of chromatin-based processes: mind the TRRAP

INO80 subfamily of chromatin remodeling complexes

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