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Mapping the local protein interactome of the NuA3 histone acetyltransferase by Sherri K. Smart; Samuel G. Mackintosh; Ricky D. Edmondson; Sean D. Taverna; Alan J. Tackett is a scholarly article available to read on EtoBox.

What is Mapping the local protein interactome of the NuA3 histone acetyltransferase about?

## Abstract 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.

Author

Sherri K. Smart; Samuel G. Mackintosh; Ricky D. Edmondson; Sean D. Taverna; Alan J. Tackett

Publisher

Cold Spring Harbor Laboratory Press; Wiley (John Wiley & Sons); Wiley-Blackwell; Wiley (ISSN 0961-8368)

Published

2009

Language

EN