Proteomic analysis of acetylation in thermophilic Geobacillus kaustophilus

Authors

  • Dong-Woo Lee,

    1. Superbacteria Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon, Korea
    2. School of Applied Biosciences, Kyungpook National University, Daegu, Korea
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    • These authors contributed equally to this work.

  • Dooil Kim,

    1. Superbacteria Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon, Korea
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    • These authors contributed equally to this work.

  • Yong-Jik Lee,

    1. Superbacteria Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon, Korea
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  • Jung-Ae Kim,

    1. Superbacteria Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon, Korea
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  • Ji Young Choi,

    1. Biomedical Proteomics Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon, Korea
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  • Sunghyun Kang,

    1. Biomedical Proteomics Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon, Korea
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  • Jae-Gu Pan

    Corresponding author
    • Superbacteria Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon, Korea
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Correspondence: Dr. Jae-Gu Pan, Superbacteria Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon 305–806, Korea

E-mail: jgpan@kribb.re.kr

Fax: +82-42-860-4488

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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