Journal
PROTEOMICS
Volume 13, Issue 15, Pages 2278-2282Publisher
WILEY-BLACKWELL
DOI: 10.1002/pmic.201200072
Keywords
Acetylation; Geobacillus kaustophilus; Microbiology; Posttranslational modification; Proteome
Funding
- 21C Frontier R&D Program of the Microbial Genomics and Applications Center [MF05-0204-2-0]
- Ministry of Science and Technology of Korea
- KRIBB Innovation Project
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Recent analysis of prokaryotic N-epsilon -lysine-acetylated proteins highlights the posttranslational regulation of a broad spectrum of cellular proteins. However, the exact role of acetylation remains unclear due to a lack of acetylated proteome data in prokaryotes. Here, we present the N-epsilon -lysine-acetylated proteome of gram-positive thermophilic Geobacillus kaustophilus. Affinity enrichment using acetyl-lysine-specific antibodies followed by LC-MS/MS analysis revealed 253 acetylated peptides representing 114 proteins. These acetylated proteins include not only common orthologs from mesophilic Bacillus counterparts, but also unique G. kaustophilus proteins, indicating that lysine acetylation is pronounced in thermophilic bacteria. These data complement current knowledge of the bacterial acetylproteome and provide an expanded platform for better understanding of the function of acetylation in cellular metabolism.
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