Bacterial GCN5-Related N-Acetyltransferases: From Resistance to Regulation.
Bacterial GCN5-Related N-Acetyltransferases: From Resistance to Regulation.
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DOI：
10.1021/acs.biochem.5b01269
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发表时间：
2016-02-23
期刊：
影响因子：
2.9
通讯作者：
Vergnolle O
中科院分区：
文献类型：
--
作者：
Favrot L;Blanchard JS;Vergnolle O
GCN 5相关的N-乙酰基转移酶家族（GNAT）是一个重要的蛋白质家族，在真核生物和原核生物中包括超过10万个成员。乙酰化作为一种主要的调节性翻译后修饰出现，并且与磷酸化一样广泛。N-乙酰转移酶将乙酰基从乙酰辅酶A转移到大量底物，从小分子如氨基糖苷类抗生素到大分子。蛋白质的乙酰化可以发生在两个不同的位置，在氨基末端（α N-乙酰化）或在内部赖氨酸残基的ε-氨基（ε N-乙酰化）。GNAT成员已根据其底物特异性分为不同的组，尽管一级序列同一性非常低，但GNAT蛋白显示出共同和保守的折叠。本主题综述了不同种类的细菌GNAT蛋白，它们的功能，结构特征和作用机制。
The GCN5-related N-acetyltransferases family (GNAT) is an important family of proteins that includes more than 100000 members among eukaryotes and prokaryotes. Acetylation appears as a major regulatory post-translational modification and is as widespread as phosphorylation. N-Acetyltransferases transfer an acetyl group from acetyl-CoA to a large array of substrates, from small molecules such as aminoglycoside antibiotics to macromolecules. Acetylation of proteins can occur at two different positions, either at the amino-terminal end (αN-acetylation) or at the ε-amino group (εN-acetylation) of an internal lysine residue. GNAT members have been classified into different groups on the basis of their substrate specificity, and in spite of a very low primary sequence identity, GNAT proteins display a common and conserved fold. This Current Topic reviews the different classes of bacterial GNAT proteins, their functions, their structural characteristics, and their mechanism of action.