Abstract:
:Ubiquitylation of histone H2B at lysine residue 120 (H2BK120ub) is a prominent histone posttranslational modification (PTM) associated with the actively transcribed genome. Although H2BK120ub triggers several critical downstream histone modification pathways and changes in chromatin structure, less is known about the regulation of the ubiquitylation reaction itself, in particular with respect to the modification status of the chromatin substrate. Here we employ an unbiased library screening approach to profile the impact of pre-existing chromatin modifications on de novo ubiquitylation of H2BK120 by the cognate human E2:E3 ligase pair, UBE2A:RNF20/40. Deposition of H2BK120ub is found to be highly sensitive to PTMs on the N-terminal tail of histone H2A, a crosstalk that extends to the common histone variant H2A.Z. Based on a series of biochemical and cell-based studies, we propose that this crosstalk contributes to the spatial organization of H2BK120ub on gene bodies, and is thus important for transcriptional regulation.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Wojcik F,Dann GP,Beh LY,Debelouchina GT,Hofmann R,Muir TWdoi
10.1038/s41467-018-03895-5subject
Has Abstractpub_date
2018-04-11 00:00:00pages
1394issue
1issn
2041-1723pii
10.1038/s41467-018-03895-5journal_volume
9pub_type
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