Dataset Information

Dynamic protein phosphorylation in Streptococcus pyogenes during growth, stationary phase and starvation

ABSTRACT: The proteome and phosphoproteome of Streptococcus pyogenes M49 was investigated at different growth phases of cultures grown in either rich medium (THY), chemically defined medium without carbon source, or chemically defined medium containing 1% fructose. Of the 815 phosphosites identified, 463 were included in a label-free quantitative analysis of dynamic protein phosphorylation. A small group of phosphorylation events, almost exclusively at threonine residues, was strongest during growth and decreased during stationary phase. These included phosphorylation sites of the PASTA kinase SP-STK and its putative substrates suggesting that the PASTA kinase-dependent processes regulating the cell cycle in related bacteria are also conserved in S. pyogenes. Most phosphorylation events occurred preferentially at serine residues in the stationary growth phase and under starvation conditions. The elucidation of the physiological significance and the responsible kinases of these phosphorylations require further investigations. In addition to phosphorylation events at S/T/Y residues, phosphoglycerylation of lysine (PGK) occurred frequently among the enriched phosphopeptides.

INSTRUMENT(S): Synapt MS

ORGANISM(S): Streptococcus Pyogenes Nz131 Bacteria

SUBMITTER: Stefan Mikkat

LAB HEAD: Stefan Mikkat

PROVIDER: PXD044423 | Pride | 2024-05-22

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	02092021_Spy_3dstat_total_HDMSe.DerivedFromSearcheda22a02-d80f-4b10-a534-b9165e043238.mgf	Mgf
	02092021_Spy_3dstat_total_HDMSe.mzid.gz	Mzid
	02092021_Spy_THY08_HDMSe_01.raw.zip	Raw
	02092021_Spy_THY08_HDMSe_02.raw.zip	Raw
	02092021_Spy_THY08_HDMSe_03.raw.zip	Raw

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Dynamic Protein Phosphorylation in <i>Streptococcus pyogenes</i> during Growth, Stationary Phase, and Starvation.

Mikkat Stefan S Kreutzer Michael M Patenge Nadja N

Microorganisms 20240320 3

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 wit ...[more]

PMID: 38543672

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