# Dynamic Protein Phosphorylation in Streptococcus pyogenes during Growth, Stationary Phase, and Starvation

**Authors:** Stefan Mikkat, Michael Kreutzer, Nadja Patenge

PMC · DOI: 10.3390/microorganisms12030621 · Microorganisms · 2024-03-20

## TL;DR

This study explores how protein phosphorylation changes in Streptococcus pyogenes under various growth conditions, revealing patterns linked to cell cycle and stationary phase.

## Contribution

The study identifies dynamic phosphorylation patterns in S. pyogenes, highlighting conserved PASTA kinase roles and potential general bacterial physiology features.

## Key findings

- A small group of phosphorylation events is linked to cell cycle proteins and occurs mainly in growing cells.
- Most phosphorylation events occur during stationary phase or starvation, preferentially at serine residues.
- PASTA kinase-dependent regulation in S. pyogenes suggests conserved mechanisms from related bacteria.

## Abstract

Phosphorylation of proteins at serine, threonine, and tyrosine residues plays an important role in physiological processes of bacteria, such as cell cycle, metabolism, virulence, dormancy, and stationary phase functions. Little is known about the targets and dynamics of protein phosphorylation in Streptococcus pyogenes, which possesses a single known transmembrane serine/threonine kinase belonging to the class of PASTA kinases. A proteomics and phosphoproteomics workflow was performed with S. pyogenes serotype M49 under different growth conditions, stationary phase, and starvation. The quantitative analysis of dynamic phosphorylation, which included a subset of 463 out of 815 identified phosphorylation sites, revealed two main types of phosphorylation events. A small group of phosphorylation events occurred almost exclusively at threonine residues of proteins related to the cell cycle and was enhanced in growing cells. The majority of phosphorylation events occurred during stationary phase or starvation, preferentially at serine residues. PASTA kinase-dependent cell cycle regulation processes found in related bacteria are conserved in S. pyogenes. Increased protein phosphorylation during the stationary phase has also been described for some other bacteria, and could therefore be a general feature in the physiology of bacteria, whose functions and the kinases involved need to be elucidated in further analyses.

## Linked entities

- **Species:** Streptococcus pyogenes (taxon 1314)

## Full-text entities

- **Species:** Streptococcus pyogenes (species) [taxon 1314], Streptococcus pyogenes serotype M49 (serotype) [taxon 301452]

## Full text

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## Figures

6 figures with captions in the complete paper: https://tomesphere.com/paper/PMC10975399/full.md

## References

83 references — full list in the complete paper: https://tomesphere.com/paper/PMC10975399/full.md

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Source: https://tomesphere.com/paper/PMC10975399