Bacterial protein acetylation: the dawning of a new age

Hu, Linda I.; Lima, Bruno P.; Wolfe, Alan J.

doi:10.1111/j.1365-2958.2010.07204.x

Cited by 154 publications

(154 citation statements)

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“…Acetylation was originally identified as a modification of histone proteins in eukaryotes, but recently similarly acetylated proteins were identified in prokaryotes reviewed by Soppa [17] and Jones and O’Connor [18]. Nε-Lysine acetylation of proteins is effected by acetyl CoA synthase and a Gcn-5-like acetyltransferase (GNAT) that uses acetyl CoA as the acetyl donor with the concomitant release of CoA [19]. The modification is reversed by a deacetylase, and the bacterial CobB sirtuin was identified as responsible for this function [20].…”

Section: Discussionmentioning

confidence: 99%

Post-translational regulation of a Porphyromonas gingivalis regulator

Krishnan

Duncan³

2018

Journal of Oral Microbiology

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Background: Bacteria use two-component signal transduction systems (among others) to perceive and respond to environmental changes. Within the genus Porphyromonas, we observed degeneration of these systems, as exemplified by the loss of RprX, the sensor kinase partner of the RprY.Objective: The purpose of this study was to investigate modulation of RprY function by acetylation.Design: The transcriptional activity of the rprY-pat genes were measured by RT-PCR and 5ʹ-RACE. The acetylation of RprY were detected by western blotting. Electromobility shift and in vitro ChIP assays were used to measure the DNA binding activity of RprY. The expression of RprY target genes was measured by qRT-PCR. Effects of acetylation on phosphorylation of RprY were measured by Phos-tag gels.Results: The rprY gene is cotranscribed with pat. RprY is acetylated in vivo, and autoacetylated in vitro in a reaction that is enhanced by Pat; the CobB sirtuin deacetylates RprY. Acetylation reduced the DNA binding of RprY. Induced oxidative stress decreased production of RprY in vivo, increased its acetylation and increased expression of nqrA.Conclusions: We propose that to compensate for the loss of RprX, P. gingivalis has evolved a novel mechanism to inactivate RprY through acetylation.

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Section: Discussionmentioning

confidence: 99%

Post-translational regulation of a Porphyromonas gingivalis regulator

Krishnan

Duncan³

2018

Journal of Oral Microbiology

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“…When induced, this pathway restores pyruvate and lactate excretion to WT levels (31). Finally, of course, (iv) AcCoA can regulate protein function by donating its acetyl group to lysine residues (32,33).…”

Section: Discussionmentioning

confidence: 99%

Inhibition of Acetyl Phosphate-dependent Transcription by an Acetylatable Lysine on RNA Polymerase

Lima

Huyền

Bäsell

et al. 2012

Journal of Biological Chemistry

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“…The model organisms E. coli and S. enterica encode ϳ26 GNAT homologues, only half of which have known or predicted functions ( Table 2). These GNATs target primary amines (80,81), including the N termini of proteins (82,83), aminoglycoside antibiotics (63), polyamines (84), a nucleotide sugar (85), glutamate (86), toxic aminoacyl nucleotides (87), and transfer RNAs (88). Three GNAT enzymes, RimI, RimJ, and RimL, acetylate the ␣-amine group at the N terminus of the ribosomal proteins S18, S5, and L12, respectively (89,90).…”

Section: Bacterial Gcn5-related N-acyltransferasesmentioning

confidence: 99%

Acylation of Biomolecules in Prokaryotes: a Widespread Strategy for the Control of Biological Function and Metabolic Stress

Hentchel

Escalante‐Semerena

2015

Microbiol Mol Biol Rev

168

175

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SUMMARY Acylation of biomolecules (e.g., proteins and small molecules) is a process that occurs in cells of all domains of life and has emerged as a critical mechanism for the control of many aspects of cellular physiology, including chromatin maintenance, transcriptional regulation, primary metabolism, cell structure, and likely other cellular processes. Although this review focuses on the use of acetyl moieties to modify a protein or small molecule, it is clear that cells can use many weak organic acids (e.g., short-, medium-, and long-chain mono- and dicarboxylic aliphatics and aromatics) to modify a large suite of targets. Acetylation of biomolecules has been studied for decades within the context of histone-dependent regulation of gene expression and antibiotic resistance. It was not until the early 2000s that the connection between metabolism, physiology, and protein acetylation was reported. This was the first instance of a metabolic enzyme (acetyl coenzyme A [acetyl-CoA] synthetase) whose activity was controlled by acetylation via a regulatory system responsive to physiological cues. The above-mentioned system was comprised of an acyltransferase and a partner deacylase. Given the reversibility of the acylation process, this system is also referred to as r eversible l ysine a cylation (RLA). A wealth of information has been obtained since the discovery of RLA in prokaryotes, and we are just beginning to visualize the extent of the impact that this regulatory system has on cell function.

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Bacterial protein acetylation: the dawning of a new age

Cited by 154 publications

References 69 publications

Post-translational regulation of a Porphyromonas gingivalis regulator

Post-translational regulation of a Porphyromonas gingivalis regulator

Inhibition of Acetyl Phosphate-dependent Transcription by an Acetylatable Lysine on RNA Polymerase

Acylation of Biomolecules in Prokaryotes: a Widespread Strategy for the Control of Biological Function and Metabolic Stress

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