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Heterochromatin protein 1 is extensively decorated with histone code-like post-translational modifications.

Authors
  • LeRoy, Gary
  • Weston, John T
  • Zee, Barry M
  • Young, Nicolas L
  • Plazas-Mayorca, Mariana D
  • Garcia, Benjamin A
Type
Published Article
Journal
Molecular & Cellular Proteomics
Publisher
American Society for Biochemistry and Molecular Biology
Publication Date
Nov 01, 2009
Volume
8
Issue
11
Pages
2432–2442
Identifiers
DOI: 10.1074/mcp.M900160-MCP200
PMID: 19567367
Source
Medline
License
Unknown

Abstract

Heterochromatin protein 1 (HP1) family members (alpha, beta, and gamma) bind histone H3 methylated at Lys-9, leading to gene silencing and heterochromatin formation. Several previous reports have suggested that HP1s are post-translationally modified, yet sites of modification have not yet been exhaustively determined. Here we perform the first comprehensive proteomic analysis of all HP1 isoforms using tandem mass spectrometry. Our data reveal that all HP1 isoforms are highly modified in a manner analogous to histones including phosphorylation, acetylation, methylation, and formylation, including several sites having multiple different types of modifications. Additionally, many of these modifications are found in both the chromo- and chromoshadow domains, suggesting that they may have an important role in modulating HP1 interactions or functions. These studies are the first to systematically map the abundant sites of covalent modifications on HP1 isoforms and provide the foundation for future investigations to test whether these modifications are essential in heterochromatin maintenance or other nuclear processes.

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