Zhao Zhiqiang, Xu Hang, Gong Weimin
National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences (CAS), Beijing 100101, China.
Protein Pept Lett. 2010 May;17(5):555-8. doi: 10.2174/092986610791112620.
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.
组蛋白去乙酰化酶6(HDAC6)是一种催化多种蛋白质去乙酰化的胞质酶。乙酰化微管蛋白最近被确定为HDAC6的生理底物。然而,在以前的报道中,所有体外结合和酶活性测定仅使用部分纯化的蛋白质样品完成。因此,HDAC6是否能单独与微管蛋白相互作用并催化去乙酰化仍不清楚。在本研究中,使用重组来源的HDAC6和纯化的α/β微管蛋白进行结合和酶活性测定,以消除可能的污染。结果清楚地表明,HDAC6与微管蛋白之间的相互作用独立于其他蛋白质。此外,HDAC6可以独立催化微管蛋白二聚体和微管聚合物的去乙酰化。