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The role of the Paf1 complex in controlling transcriptioncoupled histone modifications
Author(s) -
Arndt Karen M.,
Piro Anthony S.,
Mayekar Manasi K.,
Tomson Brett N.,
Wier Adam D.,
VanDemark Andrew P.,
Heisler Lawrence E.,
Gebbia Marinella,
Nislow Corey
Publication year - 2013
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.27.1_supplement.324.3
Subject(s) - rna polymerase ii , histone code , histone h2b , chromatin , histone , histone h2a , microbiology and biotechnology , histone methyltransferase , histone methylation , biology , histone h1 , nucleosome , histone octamer , computational biology , genetics , chemistry , gene , promoter , gene expression , dna methylation
Histone modifications that are deposited during transcription elongation impact the recruitment and activities of proteins that further restructure the chromatin template. The Paf1 complex (Paf1C) functions at the intersection of transcription elongation and histone modification by associating with RNA pol II and facilitating the modification of histones. We are exploring three aspects of Paf1C function in yeast: the mechanism by which it stimulates histone H2B K123 ubiquitylation, the nature of its physical interaction with RNA pol II, and its involvement in transcription termination. We have recently described a small domain within the Rtf1 subunit of Paf1C that is necessary and sufficient for promoting H2B ubiquitylation. Using a multidisciplinary approach, we are currently investigating how this histone modification domain interacts with chromatin and stimulates histone modification. In a separate study, we have recently identified a domain within Rtf1 that tethers Paf1C to RNA pol II through an interaction with the elongation factor Spt5. This interaction ensures that the diverse functions of Paf1C are properly targeted to active genes. Finally, using high‐resolution tiling array studies, we have demonstrated broad and gene‐specific effects of Paf1C on the termination of snoRNAs, revealing genes that differ in their dependence on Rtf1‐mediated histone modifications. Funded by NIH and CIHR.