期刊
JOURNAL OF PROTEOMICS
卷 79, 期 -, 页码 60-71出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.jprot.2012.12.001
关键词
Acetylome; Metabolism; Fire blight; Virulence; Type III secretion system; Exopolysaccharide
资金
- Campus Research Board, University of Illinois [10192]
- Agriculture and Food Research Initiative Competitive Grants Program from the USDA National Institute of Food and Agriculture [2010-65110-20497]
- NIDA [1F30DA026672]
- NIFA [2010-65110-20497, 581215] Funding Source: Federal RePORTER
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. (C) 2012 Elsevier B.V. All rights reserved.
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