The diversity of lysine-acetylated proteins in Escherichia coli. J Microbiol Biotechnol
Systems Microbiology Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon 305-806, Korea. Journal of Microbiology and Biotechnology
(Impact Factor: 1.53).
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 lysineacetylated 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.
Available from: Takfarinas Kentache
- "Escherichia coli 85 125 2.1 Immunoprecipitation  E. coli 91 138 2.2 Immunoprecipitation  E. coli 1000 8284 24.1 Immunoprecipitation/SCX  E. coli 349 1070 8.4 Immunoprecipitation  E. coli 170 614 3.5 Immunoprecipitation  Erwinia amylovora 96 141 2.6 Immunoprecipitation  Geobacillus kaustophilus 114 253 3.2 Immunoprecipitation  Leptospira interrogans 46 54 1 Direct MS analysis  Mycoplasma pneumoniae 221 719 34.1 Immunoprecipitation  "
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ABSTRACT: Post-translational modifications of proteins are key events in cellular metabolism and physiology regulation. Lysine acetylation is one of the best studied protein modifications in eukaryotes, but, until recently, ignored in bacteria. However, proteomic advances have highlighted the diversity of bacterial lysine-acetylated proteins. The current data support the implication of lysine acetylation in various metabolic pathways, adaptation and virulence. In this review, we present a broad overview of the current knowledge of lysine acetylation in bacteria. We emphasize particularly the significant contribution of proteomics in this field. This article is protected by copyright. All rights reserved.
Proteomics 09/2015; DOI:10.1002/pmic.201500258 · 3.81 Impact Factor
Available from: Thierry Jouenne
- "By comparing our data with some other bacterial studies on Lys acetylation        , 37% of our proteins were already described as acetylated in at least one bacterium (Table SI-3). The glyceraldehyde-3-phosphate dehydrogenase (PA14 22890) and the phosphopyruvate hydratase (PA14 17320) were characterized as acetylated in all studied bacteria, suggesting that LysAc might be required for their structure and function. "
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ABSTRACT: Protein lysine acetylation is a reversible and highly regulated post translational modification with the well demonstrated physiological relevance in eukaryotes. Recently, its important role in the regulation of metabolic processes in bacteria was highlighted. Here, we reported the lysine acetylproteome of Pseudomonas aeruginosa using a proteomic approach. We identified 430 unique peptides corresponding to 320 acetylated proteins. In addition to the proteins involved in various metabolic pathways, several enzymes contributing to the lipopolysaccharides biosynthesis were characterized as acetylated. This data set illustrated the abundance and the diversity of acetylated lysine proteins in P. aeruginosa and opens opportunities to explore the role of the acetylation in the bacterial physiology. This article is protected by copyright. All rights reserved.
This article is protected by copyright. All rights reserved.
Proteomics 04/2015; 15(13). DOI:10.1002/pmic.201500056 · 3.81 Impact Factor
Available from: Sara Castaño-Cerezo
- "Bacillus subtilis 332/185 a 4.4 N  Drosophila melanogaster 1981/1013 a,b,c 7.3 Y  Erwinia amylovora 141/96 a 2.6 N  Escherichia coli 8284/1000 a,c,e 24.1 N  1070/349 a 8.4 N  138/91 a 2.2 N  125/85 a 2.1 N  Geobacillus kaustophilus 253/114 a 3.2 N  Homo sapiens 3600/1750 a,b,e 8.7 N  Mycoplasma pneumoniae 719/221 a,e 34.1 N  Rattus novergicus 15,474/4541 a,c,e 19.6 Y  "
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ABSTRACT: Post-translational modification of proteins is a reversible mechanism of cellular adaptation to changing environmental conditions. In eukaryotes, the physiological relevance of N-ɛ-lysine protein acetylation is well demonstrated. In recent times, important roles in the regulation of metabolic processes in bacteria are being uncovered, adding complexity to cellular regulatory networks.
The aim of this mini-review is to sum up the current state-of-the-art in the regulation of bacterial physiology by protein acetylation. Current knowledge on the molecular biology aspects of known bacterial protein acetyltransferases and deacetylases will be summarized. Protein acetylation in Escherichia coli, Salmonella enterica, Bacillus subtilis, Rhodopseudomonas palustris and Mycobacterium tuberculosis, will be explained in the light of their physiological relevance. Progress in the elucidation of bacterial acetylomes and the emerging understanding of chemical acylation mechanisms will be discussed together with their regulatory and evolutionary implications. Fundamental molecular studies detailing this recently discovered regulatory mechanism pave the way for their prospective application for the construction of synthetic regulation networks.
New Biotechnology 12/2014; 31(6). DOI:10.1016/j.nbt.2014.03.002 · 2.90 Impact Factor
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