Differential lysine acetylation profiles of Erwinia amylovora strains revealed by proteomics.

Differential lysine acetylation profiles of Erwinia amylovora strains revealed by proteomics.
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DOI:
10.1016/j.jprot.2012.12.001
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发表时间:
2013-02-21
影响因子:
3.3
通讯作者:
Zhao Y
Zhao Y
中科院分区:
生物学2区
文献类型:
--
作者:
Wu X;Vellaichamy A;Wang D;Zamdborg L;Kelleher NL;Huber SC;Zhao Y

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蛋白质赖氨酸乙酰化(LysAc)最近被证明在大肠杆菌中广泛存在。大肠杆菌和沙门氏菌,并广泛调节细菌的生理和代谢。然而,植物病原细菌中的LysAc在很大程度上未知。本文首次报道了引起苹果和梨火疫病的肠杆菌Erwinia amylovora的赖氨酸乙酰组。使用通用抗赖氨酸乙酰化抗体的免疫印迹表明,生长条件强烈影响大肠杆菌中的LysAc谱。食淀粉的。还观察到两个E.已知amylovora菌株在植物中具有不同的毒力,表明蛋白质的翻译修饰在确定细菌菌株的毒力中可能是重要的。两株大肠杆菌LysAc的蛋白质组学分析Amylovora菌株鉴定了96种蛋白质中的141个LysAc位点,这些蛋白质在广泛的生物学途径中发挥作用。与以前的报道一致,44%的蛋白质参与代谢过程,包括中枢代谢、脂多糖、核苷酸和氨基酸代谢。有趣的是,第一次,几个蛋白参与E。发现与食淀粉菌毒力相关的胞外多糖,包括与食淀粉菌生物合成和III型分泌相关的蛋白质,被赖氨酸乙酰化,表明LysAc可能在细菌毒力中起主要作用。对E. amylovora和E.大肠杆菌进一步揭示了两种生物中LysAc的序列和结构共同性。总的来说,这些结果加强了蛋白质的LysAc广泛存在于细菌代谢和毒力中的概念。
Protein lysine acetylation (LysAc) has recently been demonstrated to be widespread in E. coli and Salmonella, and to broadly regulate bacterial physiology and metabolism. However, LysAc in plant pathogenic bacteria is largely unknown. Here we first report the lysine acetylome of Erwinia amylovora, an enterobacterium causing serious fire blight disease of apples and pears. Immunoblots using generic anti-lysine acetylation antibodies demonstrated that growth conditions strongly affected the LysAc profiles in E. amylovora. Differential LysAc profiles were also observed for two E. amylovora strains, known to have differential virulence in plants, indicating translational modification of proteins may be important in determining virulence of bacterial strains. Proteomic analysis of LysAc in two E. amylovora strains identified 141 LysAc sites in 96 proteins that function in a wide range of biological pathways. Consistent with previous reports, 44% of the proteins are involved in metabolic processes, including central metabolism, lipopolysaccharide, nucleotide and amino acid metabolism. Interestingly, for the first time, several proteins involved in E. amylovora virulence, including exopolysaccharide amylovoran biosynthesis- and type III secretion-associated proteins, were found to be lysine acetylated, suggesting that LysAc may play a major role in bacterial virulence. Comparative analysis of LysAc sites in E. amylovora and E. coli further revealed the sequence and structural commonality for LysAc in the two organisms. Collectively, these results reinforce the notion that LysAc of proteins is widespread in bacterial metabolism and virulence.
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