The Histone Modification Domain of Paf1 Complex Subunit Rtf1 Directly Stimulates H2B Ubiquitylation through an Interaction with Rad6

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The five-subunit yeast Paf1 complex (Paf1C) regulates all stages of transcription and is critical for the monoubiquitylation of histone H2B (H2Bub), a modification that broadly influences chromatin structure and eukaryotic transcription. Here, we show that the histone modification domain (HMD) of Paf1C subunit Rtf1 directly interacts with the ubiquitin conjugase Rad6 and stimulates H2Bub independently of transcription. We present the crystal structure of the Rtf1 HMD and use site-specific, in vivo crosslinking to identify a conserved Rad6 interaction surface. Utilizing ChIP-exo analysis, we define the localization patterns of the H2Bub machinery at high resolution and demonstrate the importance of Paf1C in targeting the Rtf1 HMD, and thereby H2Bub, to its appropriate genomic locations. Finally, we observe HMD-dependent stimulation of H2Bub in a transcription-free, reconstituted in vitro system. Taken together, our results argue for an active role for Paf1C in promoting H2Bub and ensuring its proper localization in vivo.
Publisher
CELL PRESS
Issue Date
2016-11
Language
English
Article Type
Article
Keywords

RNA-POLYMERASE-II; TRANSCRIPTIONAL ELONGATION; SACCHAROMYCES-CEREVISIAE; GENE-EXPRESSION; CRYPTIC TRANSCRIPTION; TUMOR-SUPPRESSOR; H3K4 METHYLATION; STRUCTURAL BASIS; HUMAN-CELLS; RECRUITMENT

Citation

MOLECULAR CELL, v.64, no.4, pp.815 - 825

ISSN
1097-2765
DOI
10.1016/j.molcel.2016.10.008
URI
http://hdl.handle.net/10203/219643
Appears in Collection
BS-Journal Papers(저널논문)
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