Journal
MOLECULAR CELL
Volume 51, Issue 5, Pages 662-677Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2013.07.015
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Funding
- NIH [P01-GM088409, GM067777, GM082989]
- Career Award in the Biomedical Sciences from the Burroughs Wellcome Fund
- Rita Allen Foundation Scholar Award
- University of Pennsylvania Structural Biology Training Grant [NIH GM08275]
- Howard Hughes Medical Institute
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The histone H2A-H2B heterodimer is an integral component of the nucleosome. The cellular localization and deposition of H2A-H2B into chromatin is regulated by numerous factors, including histone chaperones such as nucleosome assembly protein 1 (Nap1). We use hydrogen-deuterium exchange coupled to mass spectrometry to characterize H2A-H2B and Nap1. Unexpectedly, we find that at low ionic strength, the a helices in H2A-H2B are frequently sampling partially disordered conformations and that binding to Nap1 reduces this conformational sampling. We identify the interaction surface between H2A-H2B and Nap1 and confirm its relevance both in vitro and in vivo. We show that two copies of H2A-H2B bound to a Nap1 homodimer form a tetramer with contacts between H2B chains similar to those in the four-helix bundle structural motif. The organization of the complex reveals that Nap1 competes with histone-DNA and interhistone interactions observed in the nucleosome, thereby regulating the availability of histones for chromatin assembly.
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