RNA Polymerase II Carboxyl-terminal Domain Phosphorylation Regulates Protein Stability of the Set2 Methyltransferase and Histone H3 Di- and Trimethylation at Lysine 36

Fuchs, Stephen M.; Kizer, Kelby O.; Braberg, Hannes; Krogan, Nevan J.; Strahl, Brian D.

doi:10.1074/jbc.m111.273953

Cited by 54 publications

(62 citation statements)

References 52 publications

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“…Immunoblot analyses were performed as described (Fuchs et al, 2012) with the following exceptions. Embryos were lysed by bead-beating for 3 minutes in SUTEB buffer (1% SDS, 8M Urea, 10mM Tris pH 6.8, 10mM EDTA, 0.01% bromophenol blue).…”

Section: Methodsmentioning

confidence: 99%

Interrogating the Function of Metazoan Histones using Engineered Gene Clusters

et al. 2015

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SUMMARY Histones and their post-translational modifications influence the regulation of many DNA-dependent processes. Although an essential role for histone-modifying enzymes in these processes is well established, defining the specific contribution of individual histone residues remains a challenge because many histone-modifying enzymes have non-histone targets. This challenge is exacerbated by the paucity of suitable approaches to genetically engineer histone genes in metazoans. Here, we describe a facile platform in Drosophila for generating and analyzing any desired histone genotype, and we use it to test the in vivo function of three histone residues. We demonstrate that H4K20 is neither essential for DNA replication nor for completion of development, unlike conclusions drawn from analyses of H4K20 methyltransferases. We also show that H3K36 is required for viability and H3K27 is essential for maintenance of cellular identity during development. These findings highlight the power of engineering histones to interrogate genome structure and function in animals.

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Section: Methodsmentioning

confidence: 99%

Interrogating the Function of Metazoan Histones using Engineered Gene Clusters

et al. 2015

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“…While mono-and dimethylation of H3K36 by the Set2 catalytic domain require no other factors, H3K36me3 is dependent on full-length Set2 and its association with Pol II [115]. In particular, phosphorylation of the Pol II CTD by Ctk1 on Ser2 specifically stimulates Set2 binding [116-119] and is thought to positively affect Set2 protein stability [120]. Ctk1 is required for proper H3K36 trimethylation [115, 117, 119], which accumulates towards the 3′ ends of ORFs [63] (Fig.2).…”

Section: Influencing Nucleosome Dynamicsmentioning

confidence: 99%

Transcription-associated histone modifications and cryptic transcription

Smolle

Workman

2013

Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanism

173

161

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Eukaryotic genomes are packaged into chromatin, a highly organized structure consisting of DNA and histone proteins. All nuclear processes take place in the context of chromatin. Modifications of either DNA or histone proteins have fundamental effects on chromatin structure and function, and thus influence processes such as transcription, replication or recombination. In this review we highlight histone modifications specifically associated with gene transcription by RNA polymerase II and summarize their genomic distributions. Finally, we discuss how (mis-)regulation of these histone modifications perturbs chromatin organization over coding regions and results in the appearance of aberrant, intragenic transcription.

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“…A clue to the nature of this negative regulation comes from recent studies in budding yeast indicating that the WW and/ or cysteine-rich domains promote the degradation of Set2 when it is not bound to the phosphorylated Rpb1-CTD. 81,82 Regulation of Set2 stability is also proposed to link the PAF complex and the elongation factor Spt6 to H3K36me3, since loss of either of e988093-4 Volume 5 Issue 5 Transcription these factors reduces levels of S2-P, Set2, and H3K36me3. 70,79,81,83,84 This mechanism represents an attractive strategy for tightly coupling a histone-modifying activity to RNAP II, but how generally it is implemented remains an open question.…”

Section: H3k36 Methylation By Set2mentioning

confidence: 99%

Chromatin modification by the RNA Polymerase II elongation complex

Tanny

2014

Transcription

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Transcription elongation by RNA polymerase II (RNAP II) involves the coordinated action of numerous regulatory factors. Among these are chromatin-modifying enzymes, which generate a stereotypic and conserved pattern of histone modifications along transcribed genes. This pattern implies a precise coordination between regulators of histone modification and the RNAP II elongation complex. Here I review the pathways and molecular events that regulate co-transcriptional histone modifications. Insight into these events will illuminate the assembly of functional RNAP II elongation complexes and how the chromatin landscape influences their composition and function.

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RNA Polymerase II Carboxyl-terminal Domain Phosphorylation Regulates Protein Stability of the Set2 Methyltransferase and Histone H3 Di- and Trimethylation at Lysine 36

Cited by 54 publications

References 52 publications

Interrogating the Function of Metazoan Histones using Engineered Gene Clusters

Interrogating the Function of Metazoan Histones using Engineered Gene Clusters

Transcription-associated histone modifications and cryptic transcription

Chromatin modification by the RNA Polymerase II elongation complex

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