共 52 条
Unbiased proteomic screen for binding proteins to modified lysines on histone H3
被引:34
作者:
Chan, Doug W.
[1
]
Wang, Yi
[2
]
Wu, Meng
[3
]
Wong, Jiemin
[3
]
Qin, Jun
[2
]
Zhao, Yingming
[4
]
机构:
[1] ProTech Lab Inc, Houston, TX 77054 USA
[2] Baylor Coll Med, Ctr Mol Discovery Verna & Mars McLean, Dept Biochem & Mol Biol, Dept Mol & Cellular Biol, Houston, TX 77030 USA
[3] E China Normal Univ, Coll Life Sci, Inst Biomed Sci, Shanghai 200062, Peoples R China
[4] Univ Texas SW Med Ctr Dallas, Dept Biochem, Dallas, TX 75390 USA
来源:
基金:
美国国家卫生研究院;
关键词:
Epigenetics;
Histone code effectors;
Histone modifications;
Proteomics;
MASS-SPECTROMETRY;
POSTTRANSLATIONAL MODIFICATIONS;
CELL-CULTURE;
CHROMATIN MODIFICATIONS;
DNA METHYLATION;
GENE REPRESSION;
MECP1;
COMPLEX;
AMINO-ACIDS;
PHD FINGER;
TRANSCRIPTION;
D O I:
10.1002/pmic.200800600
中图分类号:
Q5 [生物化学];
学科分类号:
071010 ;
081704 ;
摘要:
We report a sensitive peptide pull-down approach in combination with protein identification by LC-MS/MS and qualitative abundance measurements by spectrum counting to identify proteins binding to histone H3 tail containing dimethyl lysine 4 (H3K4me2), dimethyl lysine 9 (H3K9me2), or acetyl lysine 9 (H3K9ac). Our study identified 86 nuclear proteins that associate with the histone H3 tail peptides examined, including seven known direct binders and 16 putative direct binders with conserved PHD finger, bromodomain, and WD40 domains. The reliability of our proteomic screen is supported by the fact that more than one-third of the proteins identified were previously described to associate with histone H3 tail directly or indirectly. To our knowledge, the results presented here are the most comprehensive analysis of H3K4me2, H3K9me2, and H3K9ac associated proteins and will provide a useful resource for researchers studying the mechanisms of histone code effector proteins.
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页码:2343 / 2354
页数:12
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