Histone Deacetylase 6 (HDAC6) Is an Independent Deacetylase for α-Tubulin

被引:23
|
作者
Zhao, Zhiqiang [2 ]
Xu, Hang [1 ]
Gong, Weimin [1 ]
机构
[1] Chinese Acad Sci, Natl Lab Biomacromol, Inst Biophys, Beijing 100101, Peoples R China
[2] Chinese Acad Sci, Grad Univ, Beijing 100049, Peoples R China
来源
PROTEIN AND PEPTIDE LETTERS | 2010年 / 17卷 / 05期
基金
中国国家自然科学基金;
关键词
HDAC6; tubulin; deacetylase; co-immunoprecipitation; enzymatic activity; IN-VIVO; MICROTUBULES; ACETYLATION; SIRT2;
D O I
10.2174/092986610791112620
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Histone deacetylase 6 (HDAC6) is a cytosolic enzyme that catalyzes deacetylation of several proteins. Acetylated tubulin has been recently identified as a physiological substrate of HDAC6. However in previous reports, all in vitro binding and enzymatic assays were accomplished with only partially purified protein samples. Therefore, it still remained unclear whether HDAC6 alone could interact with tubulin and catalyze deacetylation. In this study, both binding and enzymatic assays were conducted using recombinant-derived HDAC6 and purified alpha/beta tubulin to eliminate possible contamination. The results clearly demonstrated that interaction between HDAC6 and tubulin is independent of other proteins. In addition, HDAC6 can independently catalyze deacetylation of both tubulin dimer and microtubule polymer.
引用
收藏
页码:555 / 558
页数:4
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