Proteomic analysis of acetylation in thermophilic Geobacillus kaustophilus

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Title
Proteomic analysis of acetylation in thermophilic Geobacillus kaustophilus
Author(s)
Dong-Woo Lee; D Kim; Y J Lee; Jung-Ae Kim; Ji Young Choi; Sunghyun Kang; Jae Gu Pan
Bibliographic Citation
Proteomics, vol. 13, no. 15, pp. 2278-2282
Publication Year
2013
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.
Keyword
AcetylationGeobacillus kaustophilusMicrobiologyPosttranslational modificationProteomeThermophile
ISSN
1615-9853
Publisher
Wiley
DOI
http://dx.doi.org/10.1002/pmic.201200072
Type
Article
Appears in Collections:
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
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