Article

 

The Cac2 subunit is essential for productive histone binding and nucleosome assembly in CAF-1. Public Deposited

https://scholar.colorado.edu/concern/articles/z029p540v
Abstract
  • Nucleosome assembly following DNA replication controls epigenome maintenance and genome integrity. Chromatin assembly factor 1 (CAF-1) is the histone chaperone responsible for histone (H3-H4)₂ deposition following DNA synthesis. Structural and functional details for this chaperone complex and its interaction with histones are slowly emerging. Using hydrogen-deuterium exchange coupled to mass spectrometry, combined with in vitro and in vivo mutagenesis studies, we identified the regions involved in the direct interaction between the yeast CAF-1 subunits, and mapped the CAF-1 domains responsible for H3-H4 binding. The large subunit, Cac1 organizes the assembly of CAF-1. Strikingly, H3-H4 binding is mediated by a composite interface, shaped by Cac1-bound Cac2 and the Cac1 acidic region. Cac2 is indispensable for productive histone binding, while deletion of Cac3 has only moderate effects on H3-H4 binding and nucleosome assembly. These results define direct structural roles for yeast CAF-1 subunits and uncover a previously unknown critical function of the middle subunit in CAF-1.
Creator
Date Issued
  • 2017-04-18
Academic Affiliation
Journal Title
Journal Volume
  • 7
File Extent
  • 46274-46274
Last Modified
  • 2019-12-05
Identifier
  • PubMed ID: 28418026
Resource Type
Rights Statement
DOI
ISSN
  • 2045-2322
Language
License

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