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Mapping the local protein interactome of the NuA3 histone acetyltransferase
Author(s) -
Smart Sherri K.,
Mackintosh Samuel G.,
Edmondson Ricky D.,
Taverna Sean D.,
Tackett Alan J.
Publication year - 2009
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.212
Subject(s) - chromatin , interactome , histone , nucleosome , chromatin remodeling , histone h2b , microbiology and biotechnology , histone acetyltransferase , biology , p300 cbp transcription factors , chemistry , computational biology , biochemistry , dna , histone acetyltransferases , gene
Protein–protein interactions modulate cellular functions ranging from the activity of enzymes to signal transduction cascades. A technology termed transient isotopic differentiation of interactions as random or targeted (transient I‐DIRT) is described for the identification of stable and transient protein–protein interactions in vivo . The procedure combines mild in vivo chemical cross‐linking and non‐stringent affinity purification to isolate low abundance chromatin‐associated protein complexes. Using isotopic labeling and mass spectrometric readout, purified proteins are categorized with respect to the protein ‘bait’ as stable, transient, or contaminant. Here we characterize the local interactome of the chromatin‐associated NuA3 histone lysine‐acetyltransferase protein complex. We describe transient associations with the yFACT nucleosome assembly complex, RSC chromatin remodeling complex and a nucleosome assembly protein. These novel, physical associations with yFACT, RSC, and Nap1 provide insight into the mechanism of NuA3‐associated transcription and chromatin regulation.