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The nucleosome acidic patch directly interacts with subunits of the Paf1 and FACT complexes and controls chromatin architecture in vivo
Author(s) -
Christine E. Cucinotta,
A Elizabeth Hildreth,
Brendan M. McShane,
Margaret K. Shirra,
Karen M. Arndt
Publication year - 2019
Publication title -
nucleic acids research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 9.008
H-Index - 537
eISSN - 1362-4954
pISSN - 0305-1048
DOI - 10.1093/nar/gkz549
Subject(s) - nucleosome , biology , chromatin , microbiology and biotechnology , histone , histone code , chromatin structure remodeling (rsc) complex , transcription (linguistics) , histone h2b , histone octamer , rna polymerase ii , linker dna , dna , dna binding protein , protein subunit , biochemistry , transcription factor , promoter , gene expression , gene , linguistics , philosophy
The nucleosome core regulates DNA-templated processes through the highly conserved nucleosome acidic patch. While structural and biochemical studies have shown that the acidic patch controls chromatin factor binding and activity, few studies have elucidated its functions in vivo. We employed site-specific crosslinking to identify proteins that directly bind the acidic patch in Saccharomyces cerevisiae and demonstrated crosslinking of histone H2A to Paf1 complex subunit Rtf1 and FACT subunit Spt16. Rtf1 bound to nucleosomes through its histone modification domain, supporting its role as a cofactor in H2B K123 ubiquitylation. An acidic patch mutant showed defects in nucleosome positioning and occupancy genome-wide. Our results provide new information on the chromatin engagement of two central players in transcription elongation and emphasize the importance of the nucleosome core as a hub for proteins that regulate chromatin during transcription.

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