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• W2020113425 abstract "Transcription activation has been proposed to require both ubiquitylation and deubiquitylation of histone H2B. Here, we show that Lge1 (Large 1) is found in a complex containing Rad6.Bre1 and that it controls the recruitment of Bre1, a ubiquitin ligase, and Ubp8, a deubiquitylase, to promote ubiquitylation during the early steps in elongation. Chromatin immunoprecipitation experiments showed that Lge1 associates with promoter and coding regions of actively transcribed genes in a transcription-dependent manner. Disruption of Lge1 abolished ubiquitylation of histone H2B on lysine 123 and H3 methylation on lysines 4 and 79 and resulted in significant sensitivity to 6-azauracil and mycophenolic acid. In particular, in Lge1-deficient cells, Bre1 recruitment was attenuated, whereas recruitment of Ubp8 was facilitated. These alterations were coincident with changes in the interaction between Bre1.Ubp8 and RNA polymerase II phosphorylated at serine 5 of the C-terminal domain. We propose that Lge1 has a novel function in disrupting the balance between the recruitment of Bre1 and Ubp8, thus promoting transcription elongation." @default.
• W2020113425 created "2016-06-24" @default.
• W2020113425 creator A5006959325 @default.
• W2020113425 creator A5067136962 @default.
• W2020113425 date "2010-01-01" @default.
• W2020113425 modified "2023-10-12" @default.
• W2020113425 title "A Bre1-associated Protein, Large 1 (Lge1), Promotes H2B Ubiquitylation during the Early Stages of Transcription Elongation" @default.
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• W2020113425 doi "https://doi.org/10.1074/jbc.m109.039255" @default.
• W2020113425 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2807294" @default.
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