Your browser doesn't support javascript.
loading
Clostridioides difficile Phosphoproteomics Shows an Expansion of Phosphorylated Proteins in Stationary Growth Phase.
Smits, Wiep Klaas; Mohammed, Yassene; de Ru, Arnoud H; Cordo', Valentina; Friggen, Annemieke H; van Veelen, Peter A; Hensbergen, Paul J.
Afiliación
  • Smits WK; Department of Medical Microbiology, Leiden University Medical Centergrid.10419.3d, Leiden, The Netherlands.
  • Mohammed Y; Center for Proteomics and Metabolomics, Leiden University Medical Centergrid.10419.3d, Leiden, The Netherlands.
  • de Ru AH; Proteomics Centre, University of Victoria, Victoria, BC, Canada.
  • Cordo' V; Center for Proteomics and Metabolomics, Leiden University Medical Centergrid.10419.3d, Leiden, The Netherlands.
  • Friggen AH; Center for Proteomics and Metabolomics, Leiden University Medical Centergrid.10419.3d, Leiden, The Netherlands.
  • van Veelen PA; Department of Medical Microbiology, Leiden University Medical Centergrid.10419.3d, Leiden, The Netherlands.
  • Hensbergen PJ; Center for Proteomics and Metabolomics, Leiden University Medical Centergrid.10419.3d, Leiden, The Netherlands.
mSphere ; 7(1): e0091121, 2022 02 23.
Article en En | MEDLINE | ID: mdl-34986318
Phosphorylation is a posttranslational modification that can affect both housekeeping functions and virulence characteristics in bacterial pathogens. In the Gram-positive enteropathogen Clostridioides difficile, the extent and nature of phosphorylation events are poorly characterized, though a protein kinase mutant strain demonstrates pleiotropic phenotypes. Here, we used an immobilized metal affinity chromatography strategy to characterize serine, threonine, and tyrosine phosphorylation in C. difficile. We find limited protein phosphorylation in the exponential growth phase but a sharp increase in the number of phosphopeptides after the onset of the stationary growth phase. Our approach identifies expected targets and phosphorylation sites among the more than 1,500 phosphosites, including the protein kinase PrkC, the anti-sigma-F factor antagonist (SpoIIAA), the anti-sigma-B factor antagonist (RsbV), and HPr kinase/phosphorylase (HprK). Analysis of high-confidence phosphosites shows that phosphorylation on serine residues is most common, followed by threonine and tyrosine phosphorylation. This work forms the basis for a further investigation into the contributions of individual kinases to the overall phosphoproteome of C. difficile and the role of phosphorylation in C. difficile physiology and pathogenesis. IMPORTANCE In this paper, we present a comprehensive analysis of protein phosphorylation in the Gram-positive enteropathogen Clostridioides difficile. To date, only limited evidence on the role of phosphorylation in the regulation of this organism has been published; the current study is expected to form the basis for research on this posttranslational modification in C. difficile. .
Asunto(s)
Palabras clave
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Clostridioides difficile Tipo de estudio: Prognostic_studies Idioma: En Revista: MSphere Año: 2022 Tipo del documento: Article País de afiliación: Países Bajos Pais de publicación: Estados Unidos
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Clostridioides difficile Tipo de estudio: Prognostic_studies Idioma: En Revista: MSphere Año: 2022 Tipo del documento: Article País de afiliación: Países Bajos Pais de publicación: Estados Unidos