Regulation of Protein Post-Translational Modifications on Metabolism of Actinomycetes

Abstract

Protein post-translational modification (PTM) is a reversible process, which can dynamically regulate the metabolic state of cells through regulation of protein structure, activity, localization or protein–protein interactions. Actinomycetes are present in the soil, air and water, and their life cycle is strongly determined by environmental conditions. The complexity of variable environments urges Actinomycetes to respond quickly to external stimuli. In recent years, advances in identification and quantification of PTMs have led researchers to deepen their understanding of the functions of PTMs in physiology and metabolism, including vegetative growth, sporulation, metabolite synthesis and infectivity. On the other hand, most donor groups for PTMs come from various metabolites, suggesting a complex association network between metabolic states, PTMs and signaling pathways. Here, we review the mechanisms and functions of PTMs identified in Actinomycetes, focusing on phosphorylation, acylation and protein degradation in an attempt to summarize the recent progress of research on PTMs and their important role in bacterial cellular processes.

Post-translational Modifications in Oral Bacteria and Their Functional Impact

“…Protein tyrosine phosphorylation is catalyzed by the tyrosine (BY) kinase family, which has thus far been identified only in bacteria ( Mijakovic et al, 2016 ). A BY kinase possesses a transmembrane domain that can function not only as a kinase anchor but also as a sensor domain and an intracellular catalytic domain that binds ATP and transfers its phosphate to the hydroxyl unit of the tyrosine residue ( Sun et al, 2020 ). The catalytic domain is defined by the canonical Walker A (P-loop) and B motif.…”

Modulation of Gene Expression in Actinobacteria by Translational Modification of Transcriptional Factors and Secondary Metabolite Biosynthetic Enzymes

“…Many proteins are crotonylated rather than acetylated in S. roseosporus. Using a mutant of S. roseosporus deleted in the gene encoding the Kct1 acetyltransferase, Sun et al (2020a , b) found low protein crotonylation during the mutant growth phase. This finding suggests that this enzyme is partially responsible for the crotonylation reaction; however, there were no differences in the amount of crotonylated proteins during the late differentiation and secondary metabolites production phases between the parental strain and the Kct1 mutant.…”

“…Streptomyces Glk can be crotonylated, and this effect is reversed by the activities of decrotonylase CobB and the crotonyl-transferase Kct1 to negatively control its activity ( Sun et al, 2020a ). Furthermore, crotonylation positively regulates CCR for Streptomyces metabolism by modulating the ratio of glucose uptake/Glk activity and allowing other carbon sources utilization.…”

Protein acylation links metabolism and the control of signal transduction, transcription regulation, growth, and pathogenicity in Actinobacteria

“…As a classic PTM, protein acetylation consists of two processes: (1) the transfer of acetyl moieties to protein substrates via acetyltransferase‐dependent or nonenzymatic mechanisms (Narita et al, 2019; Sun, Li, et al, 2020; Wolfe, 2016) and (2) the removal of acetyl groups by deacetylases (Christensen et al, 2018; Sun, Li, et al, 2020; VanDrisse & Escalante‐Semerena, 2019). Notably, not all acetylated lysines are sensitive to the corresponding deacetylase.…”