Transcription-linked acetylation by Gcn5p of histones H3 and H4 at specific lysines

Kuo, Min-Liang; Brownell, James E.; Sobel, Richard; Ranalli, Tamara A.; Cook, Richard G.; Edmondson, Diane G.; Roth, Sharon Y.; Allis, C. David

doi:10.1038/383269a0

Cited by 562 publications

(535 citation statements)

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“…One obvious possibility is the SAGA complex. This complex contains ADA2, which can interact with the GAL4 activation domain in vitro (49), and GCN5, which can acetylate the histone H3 and H4 amino termini, possibly altering chromatin structure in a way that facilitates transcription factor access (26,42). This idea is buttressed by studies showing that recruitment of the SAGA complex by the VP16 and GCN4 activation domains can allow transcriptional activation of nucleosomal templates in vitro (72).…”

Section: Retention Of Tbp Function In a Gal4-tbp Fusionmentioning

confidence: 80%

Artificially Recruited TATA-Binding Protein Fails To Remodel Chromatin and Does Not Activate Three Promoters That Require Chromatin Remodeling

Ryan

Stafford

et al. 2000

Molecular and Cellular Biology

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Transcriptional activators are believed to work in part by recruiting general transcription factors, such as TATA-binding protein (TBP) and the RNA polymerase II holoenzyme. Activation domains also contribute to remodeling of chromatin in vivo. To determine whether these two activities represent distinct functions of activation domains, we have examined transcriptional activation and chromatin remodeling accompanying artificial recruitment of TBP in yeast (Saccharomyces cerevisiae). We measured transcription of reporter genes with defined chromatin structure by artificial recruitment of TBP and found that a reporter gene whose TATA element was relatively accessible could be activated by artificially recruited TBP, whereas two promoters, GAL10 and CHA1, that have accessible activator binding sites, but nucleosomal TATA elements, could not. A third reporter gene containing the HIS4 promoter could be activated by GAL4-TBP only when a RAP1 binding site was present, although RAP1 alone could not activate the reporter, suggesting that RAP1 was needed to open the chromatin structure to allow activation. Consistent with this interpretation, artificially recruited TBP was unable to perturb nucleosome positioning via a nucleosomal binding site, in contrast to a true activator such as GAL4, or to perturb the TATA-containing nucleosome at the CHA1 promoter. Finally, we show that activation of the GAL10 promoter by GAL4, which requires chromatin remodeling, can occur even in swi gcn5 yeast, implying that remodeling pathways independent of GCN5, the SWI-SNF complex, and TFIID can operate during transcriptional activation in vivo.Transcriptional activators are thought to stimulate transcription of TATA-containing promoters in part by recruiting TFIID, a multiprotein complex consisting of the TATA-binding protein (TBP) and TBP-associated factors (TAFs), to the TATA box (25,60). Several in vitro and in vivo studies support this model. For example, transcription initiated at a mutated TATA element by induced synthesis of TBP with altered specificity was enhanced in both rate and extent in the presence of an activator that could bind upstream of the relevant promoter, consistent with activator-mediated recruitment (40). Recruitment has also been inferred from the results of "activator bypass" experiments in which artificial recruitment of TBP to promoter sites near the TATA element resulted in transcriptional activation, implying that TBP recruitment is a rate-limiting step in transcriptional activation in vivo (10,39,79). Most convincingly, chromatin immunoprecipitation experiments revealed TBP to be physically associated with promoters of numerous genes under activated, but not nonactivated, conditions, implying that recruitment accompanies activation (43,46).A potential obstacle to recruitment of TBP in vivo is posed by chromatin. Binding of TBP to nucleosomal TATA elements is greatly impeded in vitro (23, 32). Transcription is also strongly repressed by chromatin, but this repression can be largely alleviated by binding of act...

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Section: Retention Of Tbp Function In a Gal4-tbp Fusionmentioning

confidence: 80%

Artificially Recruited TATA-Binding Protein Fails To Remodel Chromatin and Does Not Activate Three Promoters That Require Chromatin Remodeling

Ryan

Stafford

et al. 2000

Molecular and Cellular Biology

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“…Meanwhile, many reports have been reported on regulation of transcription by histone acetyltransferases (HAT) (Struhl, 1998), such as p300/CBP (Ogryzko et al, 1996;Bannister and Kouzarides, 1996), P/CAF (Ogryzko et al, 1996), TAFII250 (Imhof et al, 1997), and GCN5 (Kuo et al, 1996;Wang et al, 1997). These HATs acetylate not only histones but also certain transcription factors, such as p53 by p300 and P/CAF (Gu and Roeder, 1997;Sakaguchi et al, 1998), TFIIF and TFIIE by p300/CBP, P/CAF, and TAFII250 (Imhof et al, 1997), erythroid KruÈ ppel-like factor (EKLF) by p300/CBP (Zhang and Bieker, 1998), GATA-1 by CBP (Boyes et al, 1998;Hung et al, 1999), and Drosophila T-cell factor (dTCF) by dCBP (Waltzer and Bienz, 1998).…”

Section: Introductionmentioning

confidence: 99%

c-Myb acetylation at the carboxyl-terminal conserved domain by transcriptional co-activator p300

et al. 2000

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“…In Drosophila, lysines 14 and 23 are the predominant sites of acetylation, whereas in Tetrahymena, lysines 9 and 14 are preferred (10). In budding yeast, new H3 is mostly monoacetylated on lysine 9, although lysines 9, 14, 23, and 27 all show some acetylation (13). It is currently unknown whether the acetylation marks in the N-terminal tails of the newly synthesized histone H3 are removed rapidly following chromatin assembly, as is the case for H4.…”

mentioning

confidence: 96%

The Histone Chaperone Anti-silencing Function 1 Stimulates the Acetylation of Newly Synthesized Histone H3 in S-phase

Adkins

Carson

English

et al. 2007

Journal of Biological Chemistry

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Anti-silencing function 1 (Asf1) is a highly conserved chaperone of histones H3/H4 that assembles or disassembles chromatin during transcription, replication, and repair. We have found that budding yeast lacking Asf1 has greatly reduced levels of histone H3 acetylated at lysine 9. Lysine 9 is acetylated on newly synthesized budding yeast histone H3 prior to its assembly onto newly replicated DNA. Accordingly, we found that the vast majority of H3 Lys-9 acetylation peaked in S-phase, and this S-phase peak of H3 lysine 9 acetylation was absent in yeast lacking Asf1. By contrast, deletion of ASF1 has no effect on the S-phase specific peak of H4 lysine 12 acetylation; another modification carried by newly synthesized histones prior to chromatin assembly. We show that Gcn5 is the histone acetyltransferase responsible for the S-phase-specific peak of H3 lysine 9 acetylation. Strikingly, overexpression of Asf1 leads to greatly increased levels of H3 on acetylation on lysine 56 and Gcn5-dependent acetylation on lysine 9. Analysis of a panel of Asf1 mutations that modulate the ability of Asf1 to bind to histones H3/H4 demonstrates that the histone binding activity of Asf1 is required for the acetylation of Lys-9 and Lys-56 on newly synthesized H3. These results demonstrate that Asf1 does not affect the stability of the newly synthesized histones per se, but instead histone binding by Asf1 promotes the efficient acetylation of specific residues of newly synthesized histone H3.The eukaryotic genome is packaged into a nucleoprotein structure known as chromatin. The basic repeating unit of chromatin, the nucleosome, is made up of 147 base pairs of DNA wrapped around a histone octamer (two molecules each of histone proteins H2A, H2B, H3, and H4) (1). Chromatin provides a formidable obstacle to the cellular machinery gaining access to the DNA. Indeed, it is becoming apparent that chromatin is a highly dynamic structure that tightly regulates all nuclear processes that use DNA as a substrate; including transcription, DNA replication, repair, and recombination (2-4). Thus, the mechanisms by which chromatin structures are made and modified are fundamental questions of broad interest.The entire eukaryotic genome is assembled into chromatin following DNA replication, and this occurs in a stepwise manner; a tetramer of histones H3/H4 is deposited first followed by two dimers of H2A/H2B on the outside of the tetramer. Histone-binding proteins, termed histone chaperones, mediate chromatin assembly. It is known that when this process is coupled to DNA replication in vitro, it is mediated by the histone H3/H4 chaperone chromatin assembly factor 1 (CAF-1) 2 (5) together with another H3/H4 chaperone termed anti-silencing function 1 (Asf1) (6). CAF-1 and Asf1 have also been shown to localize to the sites of DNA replication (7, 8), supporting a role in assembling chromatin following DNA replication in vivo. The fact that CAF-1 and Asf1 co-purify with the replicationspecific histone variant H3.1 from HeLa cells is further evidence that Asf1 ...

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Transcription-linked acetylation by Gcn5p of histones H3 and H4 at specific lysines

Cited by 562 publications

References 23 publications

Artificially Recruited TATA-Binding Protein Fails To Remodel Chromatin and Does Not Activate Three Promoters That Require Chromatin Remodeling

Artificially Recruited TATA-Binding Protein Fails To Remodel Chromatin and Does Not Activate Three Promoters That Require Chromatin Remodeling

c-Myb acetylation at the carboxyl-terminal conserved domain by transcriptional co-activator p300

The Histone Chaperone Anti-silencing Function 1 Stimulates the Acetylation of Newly Synthesized Histone H3 in S-phase

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