The diversity of lysine-acetylated proteins in Escherichia coli

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Title
The diversity of lysine-acetylated proteins in Escherichia coli
Author(s)
Byung Jo Yu; Jung-Ae Kim; Jeong Hee Moon; Seong Eon Ryu; Jae Gu Pan
Bibliographic Citation
Journal of Microbiology and Biotechnology, vol. 18, no. 9, pp. 1529-1536
Publication Year
2008
Abstract
Acetylation of lysine residues in proteins is a reversible and highly regulated posttranslational modification. However, it has not been systematically studied in prokaryotes. By affinity immunoseparation using an anti-acetyllysine antibody together with nano-HPLC/MS/MS, we identified 125 lysine-acetylated sites in 85 proteins among proteins derived from Escherichia coli. The lysine-acetylated proteins identified are involved in diverse cellular functions including protein synthesis, carbohydrate metabolism, the TCA cycle, nucleotide and amino acid metabolism, chaperones, and transcription. Interestingly, we found a higher level of acetylation during the stationary phase than in the exponential phase; proteins acetylated during the stationary phase were immediately deacetylated when the cells were transferred to fresh LB culture medium. These results demonstrate that lysine acetylation is abundant in E. coli and might be involved in modifying or regulating the activities of various enzymes involved in critical metabolic processes and the synthesis of building blocks in response to environmental changes.
Keyword
escherichia coligrowth phaselysine acetylation
ISSN
1017-7825
Publisher
Korea Soc-Assoc-Inst
Type
Article
Appears in Collections:
Division of Bio Technology Innovation > Core Research Facility & Analysis Center > 1. Journal Articles
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