Mechanisms, Detection, and Relevance of Protein Acetylation in Prokaryotes

Abstract

Posttranslational modification of a protein, either alone or in combination with other modifications, can control properties of that protein, such as enzymatic activity, localization, stability, or interactions with other molecules. N-ε-Lysine acetylation is one such modification that has gained attention in recent years, with a prevalence and significance that rival those of phosphorylation. This review will discuss the current state of the field in bacteria and some of the work in archaea, focusing on both mechanisms of N-ε-lysine acetylation and methods to identify, quantify, and characterize specific acetyllysines. Bacterial N-ε-lysine acetylation depends on both enzymatic and nonenzymatic mechanisms of acetylation, and recent work has shed light into the regulation of both mechanisms. Technological advances in mass spectrometry have allowed researchers to gain insight with greater biological context by both (i) analyzing samples either with stable isotope labeling workflows or using label-free protocols and (ii) determining the true extent of acetylation on a protein population through stoichiometry measurements. Identification of acetylated lysines through these methods has led to studies that probe the biological significance of acetylation. General and diverse approaches used to determine the effect of acetylation on a specific lysine will be covered.

The Impact of ackA, pta, and ackA-pta Mutations on Growth, Gene Expression and Protein Acetylation in Escherichia coli K-12

“…Although both effects of acetyl-P have been convincingly demonstrated, their impact on cellular physiology is not fully elucidated, so far. Protein acetylation in E. coli has been studied on a global scale and acetylation of central metabolic enzymes is currently discussed as a mechanism to control metabolic fluxes (Weinert et al, 2013;Kuhn et al, 2014;Carabetta and Cristea, 2017;Nakayasu et al, 2017;Brunk et al, 2018;Christensen et al, 2019;VanDrisse and Escalante-Semerena, 2019). Besides such global effects, for a number of proteins an impact of acetylation on activity was shown (Wolfe, 2016;Carabetta and Cristea, 2017).…”

Overexpression of ATP sulfurylase improves the sulfur amino acid content, enhances the accumulation of Bowman–Birk protease inhibitor and suppresses the accumulation of the β-subunit of β-conglycinin in soybean seeds

“…www.nature.com/scientificreports/ likely that these compounds arise non-enzymatically, possibly by a reaction with acetyl-CoA. Such reactions are known to occur under relatively basic conditions within cells or in vitro 36 . It is possible that the ATP sulfurylase overexpressing seeds either contained higher levels of acetyl-CoA or that the internal pH or other conditions were more conducive for the reaction to occur.…”

Post-Translational Modifications Aid Archaeal Survival

“…For example, acetylation was long considered rare in Archaea. Recently, some studies have reported that acetylation is essential for the viability of haloarchaea [23,24]. Moreover, N-terminal protein acetylation is common in Eukaryotes and Archaea but very rare in Bacteria [25].…”