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Proteomics. 2013 Aug;13(15):2278-82. doi: 10.1002/pmic.201200072. Epub 2013 Jul 11.

Proteomic analysis of acetylation in thermophilic Geobacillus kaustophilus.

Author information

1
Superbacteria Research Center, Korea Research Institute of Bioscience and Biotechnology-KRIBB, Daejeon, Korea.

Abstract

Recent analysis of prokaryotic N(ε)-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(ε)-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.

KEYWORDS:

Acetylation; Geobacillus kaustophilus; Microbiology; Posttranslational modification; Proteome; Thermophile

PMID:
23696451
DOI:
10.1002/pmic.201200072
[Indexed for MEDLINE]

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