Acetylation by Eis and Deacetylation by Rv1151c of Mycobacterium tuberculosis HupB: Biochemical and Structural Insight.
Acetylation by Eis and Deacetylation by Rv1151c of Mycobacterium tuberculosis HupB: Biochemical and Structural Insight.
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DOI：
10.1021/acs.biochem.7b01089
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发表时间：
2018-02-06
期刊：
影响因子：
2.9
通讯作者：
Garneau-Tsodikova S
中科院分区：
文献类型：
--
作者：
Green KD;Biswas T;Pang AH;Willby MJ;Reed MS;Stuchlik O;Pohl J;Posey JE;Tsodikov OV;Garneau-Tsodikova S
细菌类核相关蛋白(NAP)对基因组的完整性和染色体的维持至关重要。细菌NAP的翻译后修饰似乎与研究得更好的哺乳动物NAP的功能相似。以前观察到结核分枝杆菌(Mtb)的组蛋白样NAP HupB被乙酰基转移酶EIS乙酰化，导致基因组重组。我们用EIS报道了HupB乙酰化的生化和结构方面。我们还发现Mtb的依赖于NAD+的Sirt家族脱乙酰酶Rv1151c在体外对HupB进行脱乙酰化，并对其脱乙酰化动力学进行了研究。我们认为EIS和Rv1151c的活性可以调节HupB的乙酰化状态，以重塑分枝杆菌染色体以响应环境变化。
Bacterial nucleoid-associated proteins (NAPs) are critical to genome integrity and chromosome maintenance. Post-translational modifications of bacterial NAPs appear to function similarly to their better studied mammalian counterparts. The histone-like NAP HupB from Mycobacterium tuberculosis (Mtb) was previously observed to be acetylated by the acetyltransferase Eis, leading to genome reorganization. We report biochemical and structural aspects of acetylation of HupB by Eis. We also found that the SirT-family NAD+-dependent deacetylase Rv1151c from Mtb deacetylated HupB in vitro and characterized the deacetylation kinetics. We propose that activities of Eis and Rv1151c could regulate the acetylation status of HupB to remodel the mycobacterial chromosome in response to environmental changes.
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