Phosphorylated Pol II CTD Recruits Multiple HDACs, Including Rpd3C(S), for Methylation-Dependent Deacetylation of ORF Nucleosomes

Govind, Chhabi K.; Qiu, Hongfang; Ginsburg, Daniel S.; Ruan, Chun; Hofmeyer, Kimberly; Hu, Cuihua; Venkatesh, Swaminathan; Workman, Jerry L.; Li, Bing; Hinnebusch, Alan G.

doi:10.1016/j.molcel.2010.07.003

Cited by 212 publications

(262 citation statements)

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“…5,14 The association but not hypophosphorylated Pol II, and that the interaction required Kin28, a Ser5 and Ser7 Pol II CTD kinase. 14 Furthermore, in vitro peptide binding assays showed that reconstituted Rpd3C(S) bound strongly to peptides phosphorylated at Ser5, and to di-phosphorylated peptides (Ser2P and Ser5P) even more so, when compared to unmodified peptides or peptides with Ser2 or 5 mutated to aspartic acid.…”

Section: Chromatin Remodeling Complexes Potentially Function Coordinamentioning

confidence: 94%

“…25 Recently, multiple studies have shown that both HATs and HDAs are co-transcriptionally recruited to coding regions. 1,5,8,14,24 The activities of these factors in coding regions have additionally been linked to the facilitation of transcription elongation. For example, acetylation by SAGA (Gcn5) and NuA4 (Esa1) in the GAL1 ORF mediates co-transcriptional histone eviction and Pol II processivity through coding regions.…”

Section: Histone Acetylation Is Inversely Correlated With Histone Occmentioning

confidence: 99%

“…Recent studies providing evidence for crosstalk between modifications, such as ubiquitination and methylation, 12,13 and for combinatorial mechanisms distinguishing recruitment from function, 4,14,15 reveal a far more complex code. In this article, we will focus on the application of one such combinatorial mechanism to the modulation of histone occupancy by co-transcriptionally recruited histone modifying and chromatin-remodeling complexes during transcription elongation.…”

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A role for phosphorylated Pol II CTD in modulating transcription coupled histone dynamics

Spain

Govind

2011

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Histone acetylation modulates histone occupancy both at promoters and in coding sequences. Based on our recent observation that HDACs in the budding yeast, Saccharomyces cerevisiae, are co-transcriptionally recruited to coding regions by elongating polymerases, we propose a model in which Pol II facilitates recruitment of chromatin remodeling complexes as well as other factors required for productive elongation.

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Section: Chromatin Remodeling Complexes Potentially Function Coordinamentioning

confidence: 94%

Section: Histone Acetylation Is Inversely Correlated With Histone Occmentioning

confidence: 99%

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A role for phosphorylated Pol II CTD in modulating transcription coupled histone dynamics

Spain

Govind

2011

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“…Ubiquitylation of H2B K123 by the Rad6-Bre1 ubiquitin conjugase-ligase proteins in yeast (11-13) is required for dimethylation and trimethylation of H3 K4 and K79 by the Set1/COMPASS and Dot1 methyltransferases, respectively (14-16). Histone H3 K4 dimethylation and trimethylation subsequently stimulate the recruitment and activity of histone acetyltransferase and deacetylase complexes, thereby governing histone acetylation patterns on genes (17)(18)(19)(20).From its position at the top of a histone modification cascade that determines the methylation and acetylation state of active chromatin, H2B monoubiquitylation and the factors that establish this mark are key regulators of gene expression. In addition to Rad6 and Bre1, the conserved Paf1 complex (Paf1C) is required for H2B K123 ubiquitylation.…”

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Small region of Rtf1 protein can substitute for complete Paf1 complex in facilitating global histone H2B ubiquitylation in yeast

Piro

Mayekar

Warner

et al. 2012

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

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Histone modifications regulate transcription by RNA polymerase II and maintain a balance between active and repressed chromatin states. The conserved Paf1 complex (Paf1C) promotes specific histone modifications during transcription elongation, but the mechanisms by which it facilitates these marks are undefined. We previously identified a 90-amino acid region within the Rtf1 subunit of Paf1C that is necessary for Paf1C-dependent histone modifications in Saccharomyces cerevisiae. Here we show that this histone modification domain (HMD), when expressed as the only source of Rtf1, can promote H3 K4 and K79 methylation and H2B K123 ubiquitylation in yeast. The HMD can restore histone modifications in rtf1Δ cells whether or not it is directed to DNA by a fusion to a DNA binding domain. The HMD can facilitate histone modifications independently of other Paf1C subunits and does not bypass the requirement for Rad6-Bre1. The isolated HMD localizes to chromatin, and this interaction requires residues important for histone modification. When expressed outside the context of fulllength Rtf1, the HMD associates with and causes Paf1C-dependent histone modifications to appear at transcriptionally inactive loci, suggesting that its function has become deregulated. Finally, the Rtf1 HMDs from other species can function in yeast. Our findings suggest a direct and conserved role for Paf1C in coupling histone modifications to transcription elongation.transcription-coupled histone modifications | nucleosome I n eukaryotes, transcription occurs within the context of a restrictive, yet dynamic, chromatin environment. The posttranslational modification of histones represents a major mechanism by which cells control the structure of chromatin. Some modifications of histones include acetylation, methylation, and ubiquitylation. These modifications can alter the structural properties of nucleosomes and serve as specific effectors for the recruitment of proteins that further modify the chromatin template and regulate transcription (1).Monoubiquitylation of histone H2B on lysine (K) 123 in Saccharomyces cerevisiae is a conserved modification that is enriched on active genes but plays roles in both transcriptional repression and activation (2-4). Consistent with a repressive role, H2B monoubiquitylation stabilizes nucleosomes at yeast promoters (5), inhibits the association of the RNA polymerase (pol) II kinase Ctk1 with genes in yeast (6), and interferes with the recruitment of the elongation factor TFIIS to genes in human cells (7). In other studies, H2B monoubiquitylation has been shown to stimulate transcription of chromatin templates (8), promote nucleosome reassembly during transcription elongation (9), and inhibit chromatin compaction (10). H2B monoubiquitylation is also a prerequisite for other histone modifications that mark active genes. Ubiquitylation of H2B K123 by the Rad6-Bre1 ubiquitin conjugase-ligase proteins in yeast (11-13) is required for dimethylation and trimethylation of H3 K4 and K79 by the Set1/COMPASS and Dot1 methy...

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RNA Polymerase II CTD Modifications: How Many Tales From a Single Tail

Napolitano

Lania

Majello

2014

Journal Cellular Physiology

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Eukaryote's RNA polymerases II (RNAPII) have the feature to contain, at the carbossi-terminal region of their largest subunit Rpb1, a unique CTD domain. Rpb1-CTD is composed of an increasing number of repetitions of the Y1 S2 P3 T4 S5 P6 S7 heptad that goes in parallel with the developmental level of organisms. Because of its composition, the CTD domain has a huge structural plasticity; virtually all the residues can be subjected to post-translational modifications and the two prolines can either be in cis or trans conformations. In light of these features, it is reasonable to think that different specific nuances of CTD modification and interacting factors take place not only on different gene promoters but also during different stages of the transcription cycle and reasonably might have a role even if the polymerase is on or off the DNA template. Rpb1-CTD domain is involved not only in regulating transcriptional rates, but also in all co-transcriptional processes, such as pre-mRNA processing, splicing, cleavage, and export. Moreover, recent studies highlight a role of CTD in DNA replication and in maintenance of genomic stability and specific CTD-modifications have been related to different CTD functions. In this paper, we examine results from the most recent CTD-related literature and give an overview of the general function of Rpb1-CTD in transcription, transcription-related and non transcription-related processes in which it has been recently shown to be involved in.

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Phosphorylated Pol II CTD Recruits Multiple HDACs, Including Rpd3C(S), for Methylation-Dependent Deacetylation of ORF Nucleosomes

Cited by 212 publications

References 52 publications

A role for phosphorylated Pol II CTD in modulating transcription coupled histone dynamics

A role for phosphorylated Pol II CTD in modulating transcription coupled histone dynamics

Small region of Rtf1 protein can substitute for complete Paf1 complex in facilitating global histone H2B ubiquitylation in yeast

RNA Polymerase II CTD Modifications: How Many Tales From a Single Tail

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