Systematic analysis of lysine acetylome reveals potential functions of lysine acetylation in Shewanellabaltica, the specific spoilage organism of aquatic products

ABSTRACT: Protein lysine acetylation is a major post-translational modification and plays a critical regulatory role in almost every aspect in both eukaryotes and prokaryotes, yet there have been no data on Shewanellabaltica, which is one of the specific spoilage organism (SSO) of aquatic products.Here, we performed the first global acetylproteome analysis of S. baltica. 2929 lysine acetylation sites were identified in 1103 proteins, accounting for 26.1% of the total proteins which participate in a wide variety of biological processes, especially in the constituent of ribosome, the biosynthesis of aminoacyl-tRNA, the amino acids and fatty acid metabolism. Besides, 14 conserved acetylation motifs were detected in S. baltica. Notably, various directly or indirectly spoilage-related proteins were prevalently acetylated, including enzymesinvolved in the unsaturated fatty acids biosynthesis closely related to the cold adaptability,coldshock proteins,pivotal enzymesinvolved in the putrescinebiosynthesis,and a LuxR-type protein in quorum sensing system. The acetylome analysis in Shewanella can supplement the database and provide new insight into uncovering the spoilagemechanisms of S. baltica. The provided dataset illuminates the potential role of reversible acetylation in S. baltica, and serves as an important resource for exploring the physiological role of lysine acetylation in prokaryotes.

INSTRUMENT(S): Q Exactive Plus

ORGANISM(S): Shewanella Baltica

TISSUE(S): Whole Body

SUBMITTER: Feifei Wang  

LAB HEAD: Linglin Fu

PROVIDER: PXD013895 | Pride | 2019-07-22

REPOSITORIES: Pride