Proteomic analysis of acetylation in thermophilic Geobacillus kaustophilus |
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Authors: | Dong‐Woo Lee Dooil Kim Yong‐Jik Lee Jung‐Ae Kim Ji Young Choi Sunghyun Kang Jae‐Gu Pan |
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Institution: | 1. Superbacteria Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), , Daejeon, Korea;2. School of Applied Biosciences, Kyungpook National University, , Daegu, Korea;3. Biomedical Proteomics Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), , Daejeon, Korea |
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Abstract: | Recent analysis of prokaryotic Nε‐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 Nε‐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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Keywords: | Acetylation Geobacillus kaustophilus Microbiology Posttranslational modification Proteome Thermophile |
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