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.
"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. "
[Show abstract][Hide abstract] 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.
"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  "
[Show abstract][Hide abstract] 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
"The prokaryotic enzymes, Pat and CobB, regulate bacterial protein lysine acetylation and deacetylation respectively (Starai et al., 2002; Starai and Escalante-Semerena, 2004; Wang et al., 2010). The balance between acetylation/deacetylation is influenced by several conditions, including switching carbon sources (e.g., from glucose to citrate), growth phase, and availability of acetylphosphate (AcP) (Yu et al., 2008; Zhang et al., 2009; Wang et al., 2010; Weinert et al., 2013a). Consensus sites that may serve as hotspots for lysine acetylation/deacetylation have been examined and, although no distinct patterns emerge, having tyrosine or histidine at site +1 frequently correlates with acetylation (Zhang et al., 2009), though not in all bacterial species examined (Kim et al., 2013). "
[Show abstract][Hide abstract] ABSTRACT: Lysine modifications have been studied extensively in the nucleus, where they play pivotal roles in gene regulation and constitute one of the pillars of epigenetics. In the cytoplasm, they are critical to proteostasis. However, in the last decade we have also witnessed the emergence of mitochondria as a prime locus for post-translational modification (PTM) of lysine thanks, in large measure, to evolving proteomic techniques. Here, we review recent work on evolving set of PTM that arise from the direct reaction of lysine residues with energized metabolic thioester-coenzyme A intermediates, including acetylation, succinylation, malonylation, and glutarylation. We highlight the evolutionary conservation, kinetics, stoichiometry, and cross-talk between members of this emerging family of PTMs. We examine the impact on target protein function and regulation by mitochondrial sirtuins. Finally, we spotlight work in the heart and cardiac mitochondria, and consider the roles acetylation and other newly-found modifications may play in heart disease.
Frontiers in Physiology 09/2014; 5:301. DOI:10.3389/fphys.2014.00301 · 3.53 Impact Factor
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