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In depth characterization of the S. aureus phosphoproteome reveals new targets of Stk1

ABSTRACT: Staphylococcus aureus is the leading cause of infections worldwide and infection results in a variety of diseases. As of no surprise, phosphorylation is a major game player in signaling cascades and has been shown to be involved in S. aureus virulence. Albeit long neglected, eukaryotic-like serine/threonine kinases have been implicated in these complex signaling cascades. Due to the sub-stoichiometric nature of protein phosphorylation and a lack of suitable analysis tools, the knowledge of these cascades is however, to date, still limited. Here, were apply an optimized protocol for efficient phosphopeptide enrichment via Fe3+-IMAC followed by LC-MS/MS to get a better understanding of the impact of protein phosphorylation on the complex signaling networks involved in pathogenicity. By profiling a serine/threonine kinase and phosphatase mutant from a methicillin-resistant S. aureus mutant library, we generated the most comprehensive phosphoproteome dataset of S. aureus to date, aiding a better understanding of signaling in bacteria.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Staphylococcus Aureus (strain Usa300) Bacillus Subtilis Subsp. Subtilis Str. 168

SUBMITTER: Nadine Prust

LAB HEAD: Simone Lemeer

PROVIDER: PXD020226 | Pride | 2020-12-21

REPOSITORIES: Pride

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			Action	DRS
	20180428_OR14_Ag1_Prust001_SA_2mg_Bsubtilis_IMAC_1.raw	Raw
	20180428_OR14_Ag1_Prust001_SA_2mg_Bsubtilis_IMAC_2.raw	Raw
	20180428_OR14_Ag1_Prust001_SA_2mg_Bsubtilis_IMAC_3.raw	Raw
	20190120_OR16_Ag4_Prust001_SA_SdrE_1_FP_exp7.raw	Raw
	20190120_OR16_Ag4_Prust001_SA_SdrE_2_FP_exp7.raw	Raw

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