Principles of nucleosome recognition by chromatin factors and enzymes

Robert K. McGinty, Song Tan

Research output: Contribution to journalReview articlepeer-review

Abstract

The recent torrent of structures of chromatin complexes determined by cryoelectron microscopy provides an opportunity to discern general principles for how chromatin factors and enzymes interact with their nucleosome substrate. We find that many chromatin proteins use a strikingly similar arginine anchor and variant arginine interactions to bind to the nucleosome acidic patch. We also observe that many chromatin proteins target the H3 and H2B histone fold α1-loop1 elbows and the H2B C-terminal helix on the nucleosomal histone face. These interactions with the histones can be complemented with interactions with and distortions of nucleosomal DNA.

Original languageEnglish (US)
Pages (from-to)16-26
Number of pages11
JournalCurrent Opinion in Structural Biology
Volume71
DOIs
StatePublished - Dec 2021

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Molecular Biology

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