期刊
BIOPHYSICAL CHEMISTRY
卷 136, 期 1, 页码 7-12出版社
ELSEVIER
DOI: 10.1016/j.bpc.2008.03.011
关键词
bromodomain; histone acetylation; polybromo; histone code; kinetics; protein-protein interactions
资金
- NIGMS NIH HHS [GM076055, R15 GM076055-01A2, R15 GM076055] Funding Source: Medline
Stopped-flow fluorescence anisotropy was used to determine the kinetic parameters that define acetylation-dependent bromodomain-histone interactions. Bromodomains are acetyllysine binding motifs found in many chromatin associated proteins. Individual bromodomains were derived from the polybrorno-1 protein, which is a subunit of the PBAF chromatin-remodeling complex that has six tandem bromodomains in the amino-terminal region. The average k(on) and k(off) values for the formation of high-affinity complexes are 275 M-1 s(-1) and 0.41 x 10(-3) s(-1), respectively. The average k(on) and k(off) values for the formation of low-affinity complexes are 119 M-1 s(-1) and 1.42 x 10(-3) s(-1), respectively. Analysis of the on- and off-rates yields acetylation site-dependent equilibrium dissociation constants averaging 1.4 and 12.9 mu M for high- and low-affinity complexes, respectively. This work represents the first examination of kinetic mechanisms of acetylation-dependent bromodomain-histone interactions. (C) 2008 Elsevier B.V. All rights reserved.
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