期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 285, 期 41, 页码 31337-31347出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M110.155788
关键词
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资金
- Ministry of Health, Labor, and Welfare of Japan
- Ministry of Education, Culture, Sports, Science, and Technology of Japan
- Japan Heart Foundation
- Japan Cardiovascular Research Foundation
- Japan Society for the Promotion of Science
- Mochida Memorial Foundation for Medical and Pharmaceutical Research
- Japan Medical Association
- Japan Incurable Diseases Research Foundation
- Osaka Medical Research Foundation for Incurable Diseases
- Suzuken Memorial Foundation
- Japan China Medical Association
- Grants-in-Aid for Scientific Research [22590817] Funding Source: KAKEN
Three mammalian isoforms of heterochromatin protein 1 (HP1), alpha, beta, and gamma, play diverse roles in gene regulation. Despite their structural similarity, the diverse functions of these isoforms imply that they are additionally regulated by post-translational modifications. Here, we have identified intermolecular disulfide bond formation of HP1 cysteines in an isoform-specific manner. Cysteine 133 in HP1 alpha and cysteine 177 in HP1 gamma were involved in intermolecular homodimerization. Although both HP1 alpha and HP1 gamma contain reactive cysteine residues, only HP1 gamma readily and reversibly formed disulfide homodimers under oxidative conditions. Oxidatively dimerized HP1 gamma strongly and transiently interacted with TIF1 beta, a universal transcriptional co-repressor. Under oxidative conditions, HP1 gamma dimerized and held TIF1 beta in a chromatin component and inhibited its repression ability. Our results highlight a novel, isoform-specific role for HP1 as a sensor of the cellular redox state.
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