Bacterial protein acetylation: new discoveries unanswered questions

被引：65

作者：

Wolfe, Alan J. ^{[1
]}

机构：

[1] Loyola Univ Chicago, Stritch Sch Med, Dept Microbiol & Immunol, 2160 S First Ave,Bldg 105, Maywood, IL 60153 USA

来源：

CURRENT GENETICS | 2016年 / 62卷 / 02期

关键词：

Acetyl phosphate; Acetyltransferase; CRP; Deacetylase; Metabolism; Post-translational modification; RESPONSE REGULATOR CHEY; ACID STRESS-RESPONSE; LYSINE ACETYLATION; ESCHERICHIA-COLI; COA SYNTHETASE; HISTONE DEACETYLASES; SALMONELLA-ENTERICA; PHOSPHATE; CHEMOTAXIS; COBB;

D O I：

10.1007/s00294-015-0552-4

中图分类号：

Q3 [遗传学];

学科分类号：

071007 ; 090102 ;

摘要：

N epsilon-acetylation is emerging as an abundant post-translational modification of bacterial proteins. Two mechanisms have been identified: one is enzymatic, dependent on an acetyltransferase and acetyl-coenzyme A; the other is non-enzymatic and depends on the reactivity of acetyl phosphate. Some, but not most, of those acetylations are reversed by deacetylases. This review will briefly describe the current status of the field and raise questions that need answering.

引用

页码：335 / 341

页数：7

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