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Review
. 2015 Apr:24:47-52.
doi: 10.1016/j.mib.2015.01.005. Epub 2015 Jan 24.

Ser/Thr phosphorylation as a regulatory mechanism in bacteria

Jonathan Dworkin  1
Affiliations
Review

Ser/Thr phosphorylation as a regulatory mechanism in bacteria

Jonathan Dworkin. Curr Opin Microbiol. 2015 Apr.

Abstract

This review will discuss some recent work describing the role of Ser/Thr phosphorylation as a post-translational mechanism of regulation in bacteria. I will discuss the interaction between bacterial eukaryotic-like Ser/Thr kinases (eSTKs) and two-component systems as well as hints as to physiological function of eSTKs and their cognate eukaryotic-like phosphatases (eSTPs). In particular, I will highlight the role of eSTKs and eSTPs in the regulation of peptidoglycan metabolism and protein synthesis. In addition, I will discuss how data from phosphoproteomic surveys suggest that Ser/Thr phosphorylation plays a much more significant physiological role than would be predicted simply based on in vivo and in vitro analyses of individual kinases.

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Figures

Fig. 1
Fig. 1. Regulatory phosphorylation in bacteria
A. In Two-component signaling, a Histidine kinase (HK; green) autophosphorylates in response to a signal ( formula image) and transphosphorylates a response regulator (RR; blue) on an Asp residue. B. In Ser/Thr kinase signaling, the kinase (STK; orange) undergoes autophosphorylation, presumably in response to a signal ( formula image) and transphosphorylates a substrate (Sub; blue) on Ser/Thr residue(s). A phosphatase (STP; yellow) removes these stable modifications.
Fig. 2
Fig. 2. Interaction between TCS and eSTK/eSTP systems
The response regulator (RR; blue) can be phosphorylated by the Histidine kinase (HK; green) on an Asp residue and then by a Ser/Thr kinase (STK; orange) on Ser/Thr residue(s). The Ser/Thr modifications can be reversed by a Ser/Thr phosphatase (STP; yellow).
See this image and copyright information in PMC

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