Dynamic Protein Phosphorylation in <i>Streptococcus pyogenes</i> during Growth, Stationary Phase, and Starvation
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 &l...
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| Format: | Article |
| Language: | English |
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MDPI AG
2024-03-01
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| Series: | Microorganisms |
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| Online Access: | https://www.mdpi.com/2076-2607/12/3/621 |
| _version_ | 1797239946097983488 |
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| author | Stefan Mikkat Michael Kreutzer Nadja Patenge |
| author_facet | Stefan Mikkat Michael Kreutzer Nadja Patenge |
| author_sort | Stefan Mikkat |
| collection | DOAJ |
| description | 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 <i>Streptococcus pyogenes</i>, which possesses a single known transmembrane serine/threonine kinase belonging to the class of PASTA kinases. A proteomics and phosphoproteomics workflow was performed with <i>S. pyogenes</i> 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 <i>S. pyogenes</i>. 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. |
| first_indexed | 2024-04-24T17:59:36Z |
| format | Article |
| id | doaj.art-a09f6d870f2843e9a8204c628445bcb0 |
| institution | Directory Open Access Journal |
| issn | 2076-2607 |
| language | English |
| last_indexed | 2024-04-24T17:59:36Z |
| publishDate | 2024-03-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Microorganisms |
| spelling | doaj.art-a09f6d870f2843e9a8204c628445bcb02024-03-27T13:56:01ZengMDPI AGMicroorganisms2076-26072024-03-0112362110.3390/microorganisms12030621Dynamic Protein Phosphorylation in <i>Streptococcus pyogenes</i> during Growth, Stationary Phase, and StarvationStefan Mikkat0Michael Kreutzer1Nadja Patenge2Core Facility Proteome Analysis, Rostock University Medical Center, 18057 Rostock, GermanyMedical Research Center, Rostock University Medical Center, 18057 Rostock, GermanyInstitute of Medical Microbiology, Virology and Hygiene, Rostock University Medical Center, 18057 Rostock, GermanyPhosphorylation 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 <i>Streptococcus pyogenes</i>, which possesses a single known transmembrane serine/threonine kinase belonging to the class of PASTA kinases. A proteomics and phosphoproteomics workflow was performed with <i>S. pyogenes</i> 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 <i>S. pyogenes</i>. 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.https://www.mdpi.com/2076-2607/12/3/621<i>Streptococcus pyogenes</i>phosphoproteomephosphorylation sitephosphopeptide enrichmentPASTA kinasegrowth phase |
| spellingShingle | Stefan Mikkat Michael Kreutzer Nadja Patenge Dynamic Protein Phosphorylation in <i>Streptococcus pyogenes</i> during Growth, Stationary Phase, and Starvation Microorganisms <i>Streptococcus pyogenes</i> phosphoproteome phosphorylation site phosphopeptide enrichment PASTA kinase growth phase |
| title | Dynamic Protein Phosphorylation in <i>Streptococcus pyogenes</i> during Growth, Stationary Phase, and Starvation |
| title_full | Dynamic Protein Phosphorylation in <i>Streptococcus pyogenes</i> during Growth, Stationary Phase, and Starvation |
| title_fullStr | Dynamic Protein Phosphorylation in <i>Streptococcus pyogenes</i> during Growth, Stationary Phase, and Starvation |
| title_full_unstemmed | Dynamic Protein Phosphorylation in <i>Streptococcus pyogenes</i> during Growth, Stationary Phase, and Starvation |
| title_short | Dynamic Protein Phosphorylation in <i>Streptococcus pyogenes</i> during Growth, Stationary Phase, and Starvation |
| title_sort | dynamic protein phosphorylation in i streptococcus pyogenes i during growth stationary phase and starvation |
| topic | <i>Streptococcus pyogenes</i> phosphoproteome phosphorylation site phosphopeptide enrichment PASTA kinase growth phase |
| url | https://www.mdpi.com/2076-2607/12/3/621 |
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