期刊
MOLECULAR & CELLULAR PROTEOMICS
卷 10, 期 3, 页码 -出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/mcp.M110.001198
关键词
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资金
- Rockefeller University
- Irma T. Hirschl/Monique Weill-Coulier Trust
- Ellison Medical Foundation
- NIH/NIDA [1R21DA025751-01]
- NIH/NIGMS [1R01GM087544-01A2]
- Anderson Cancer Foundation
- New York Community Trust-Heiser Grant
Bioorthogonal chemical reporters are useful tools for visualizing and identifying post-translational modifications on proteins. Here we report the proteomic analysis of mammalian proteins targeted by a series of fatty acid chemical reporters ranging from myristic to stearic acid. The large-scale analysis of total cell lysates from fully solubilized Jurkat T cells identified known fatty-acylated proteins and many new candidates, including nuclear proteins and in particular histone H3 variants. We demonstrate that histones H3.1, H3.2, and H3.3 are modified with fatty acid chemical reporters and identify the conserved cysteine 110 as a new site of S-acylation on histone H3.2. This newly discovered modification of histone H3 could have implications for nuclear organization and chromatin regulation. The unbiased proteomic analysis of fatty-acylated proteins using chemical reporters has revealed a greater diversity of lipid-modified proteins in mammalian cells and identified a novel post-translational modification of histones. Molecular & Cellular Proteomics 10: 10.1074/mcp.M110.001198, 1-16, 2011.
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