Histone H2B monoubiquitination functions cooperatively with FACT to regulate elongation by RNA polymerase II.

By Rushad Pavri, B. Zhu, Guohong Li, P. Trojer, Subhrangsu S. Mandal, A. Shilatifard, D. Reinberg. Cell, 2006

734 citations recorded by the source corpus.

Over the past years, a large number of histone posttranslational modifications have been described, some of which function to attain a repressed chromatin structure, while others facilitate activation by allowing access of regulators to DNA. Histone H2B monoubiquitination is a mark associated with transcriptional activity. Using a highly reconstituted chromatin-transcription system incorporating the inducible RARbeta2 promoter, we find that the establishment of H2B monoubiquitination by RNF20/40 and UbcH6 is dependent on the transcription elongation regulator complex PAF, the histone chaperone FACT, and transcription. H2B monoubiquitination facilitates FACT function, thereby stimulating transcript elongation and the generation of longer transcripts. These in vitro analyses and corroborating in vivo experiments demonstrate that elongation by RNA polymerase II through the nucleosomal barrier is minimally dependent upon (1) FACT and (2) the recruitment of PAF and the H2B monoubiquitination machinery.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/b0d5c0dc30d65454278985780cc80dc51bd2f993

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Citations in the corpus

Histone ubiquitination: triggering gene activity. (2008, background): “SAGA integrity is required for Ubp8 deubiquitination activity, as mutations disrupting the complex, such as spt20D, or loss of Sgf11, which is required for the association of Ubp8 with SAGA, increases the level of ubH2B (Daniel et al., 2004; Henry et al., 2003; Ingvarsdottir et al., 2005; Lee et al.”
The role of chromatin during transcription. (2007, background): “Histone H2B Monoubiquitination Histone H2B monoubiquitination (H2Bub1) occurs at both promoters and ORFs (Kao et al., 2004; Xiao et al., 2005) and is dependent on PAF and active transcription (Ng et al., 2003a; Pavri et al., 2006; Wood et al., 2003).”
Recognition of trimethylated histone H3 lysine 4 facilitates the recruitment of transcription postinitiation factors and pre-mRNA splicing. (2007, background): “In vitro analyses also established that the H3K4 trimethyl mark itself has no direct effect on transcription (Pavri et al., 2006), suggesting that H3K4me3 requires ancillary factors to carry out its effect on transcription.”
Covalent modifications of histones during development and disease pathogenesis (2007, background): “Histone H3K4 methylation does not directly affect transcription, indicating the requirement for downstream effector”
The complex language of chromatin regulation during transcription (2007, background): “There are recent examples of in vitro analysis of complex chromatin transactions, including transcriptional elongation responding to histone PTM”
Ezh1 and Ezh2 maintain repressive chromatin through different mechanisms (2008, methodology): “Chromatin Assembly and In Vitro Transcription Assays Chromatin was assembled and purified with RSF/NAP-1 as described previously (Pavri et al., 2006).”
Selective anchoring of TFIID to nucleosomes by trimethylation of histone H3 lysine 4. (2007, background): “They are supported by an elegant in vitro study using human proteins, which suggests that the H3K4me3 appears after the basal transcription machinery has assembled on the promoter (Pavri et al., 2006).”
RNF8 transduces the DNA-damage signal via histone ubiquitylation and checkpoint protein assembly. (2007, background): “In addition, monoubiquitylation of a number of proteins has been demonstrated to be responsible for protein-protein interactions (GarciaHiguera et al., 2001; Matsushita et al., 2005; Pavri et al., 2006; Stelter and Ulrich, 2003; Taniguchi et al., 2002).”