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- W2034795991 abstract "Histone H2B ubiquitination plays an important role in transcription regulation. It has been shown that H2B ubiquitination is regulated by multiple upstream events associated with elongating RNA polymerase. Here we demonstrate that H2B K34 ubiquitylation by the MOF-MSL complex is part of the protein networks involved in early steps of transcription elongation. Knocking down MSL2 in the MOF-MSL complex affects not only global H2BK34ub, but also multiple cotranscriptionally regulated histone modifications. More importantly, we show that the MSL, PAF1, and RNF20/40 complexes are recruited and stabilized at active gene promoters by direct binary interactions. The stabilized complexes serve to regulate chromatin association of pTEFb through a positive feedback loop and facilitate Pol II transition during early transcription elongation. Results from our biochemical studies are underscored by genome-wide analyses that show high RNA Pol II processivity and transcription activity at MSL target genes." @default.
- W2034795991 created "2016-06-24" @default.
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- W2034795991 date "2014-06-01" @default.
- W2034795991 modified "2023-10-14" @default.
- W2034795991 title "H2B Ubiquitylation Promotes RNA Pol II Processivity via PAF1 and pTEFb" @default.
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- W2034795991 doi "https://doi.org/10.1016/j.molcel.2014.04.013" @default.
- W2034795991 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4065619" @default.
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