Acetylome analysis of lysine acetylation in the plant pathogenic bacterium Brenneria nigrifluens. Issue 1 (2nd November 2019)

• Record Type: Journal Article
• Authors: Li, Yong; Xue, Han; Bian, Dan‐ran; Xu, Guantang; Piao, Chungen
• Is Part Of: MicrobiologyOpen. Volume 9:Issue 1(2020)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2019-11-02
• Subjects: Brenneria nigrifluens -- interaction network -- lysine acetylome -- plant pathogen -- virulence; Microbiology -- Periodicals; 579
• DOI: 10.1002/mbo3.952
• Languages: English
• ISSNs: 2045-8827

Abstract

Abstract: Protein lysine acetylation, a dynamic and reversible posttranslational modification, plays a crucial role in several cellular processes, including cell cycle regulation, metabolism, enzymatic activities, and protein interactions. Brenneria nigrifluens is a pathogen of walnut trees with shallow bark canker and can cause serious disease in walnut trees. Until now, a little has been known about the roles of lysine acetylation in plant pathogenic bacteria. In the present study, the lysine acetylome of B. nigrifluens was determined by high‐resolution LC‐MS/MS analysis. In total, we identified 1, 866 lysine acetylation sites distributed in 737 acetylated proteins. Bioinformatics results indicated that acetylated proteins participate in many different biological functions in B. nigrifluens . Four conserved motifs, namely, LK ac, K ac *F, I*K ac, and L*K ac, were identified in this bacterium. Protein interaction network analysis indicated that all kinds of interactions are modulated by protein lysine acetylation. Overall, 12 acetylated proteins were related to the virulence of B. nigrifluens . Abstract : In the present study, the lysine acetylome of Brenneria nigrifluens was determined by high‐resolution LC‐MS/MS analysis. In total, we identified 1, 866 lysine acetylation sites distributed in 737 acetylated proteins. Bioinformatics results indicate that acetylated proteins participate in many different biological functions in B. nigrifluens .