Ser/Thr/Tyr phosphoproteome analysis of pathogenic and non-pathogenic Pseudomonas species

Ayshwarya Ravichandran, Naoyuki Sugiyama, Masaru Tomita, Sanjay Swarup, Yasushi Ishihama

Research output: Contribution to journalArticle

87 Citations (Scopus)

Abstract

Protein phosphorylation on serine, threonine, and tyrosine is well established as a crucial regulatory posttranslational modification in eukaryotes. With the recent whole-genome sequencing projects reporting the presence of serine/threonine kinases and two-component proteins both in prokaryotes and eukaryotes, the importance of protein phosphorylation in archaea and bacteria is gaining acceptance. While conventional biochemical methods failed to obtain a snapshot of the bacterial phosphoproteomes, advances in MS methods have paved the way for in-depth mapping of phosphorylation sites. Here, we present phosphoproteomes of two ecologically diverse non-enteric Gram-negative bacteria captured by a nanoLC-MS-based approach combined with a novel phosphoenrichment method. While the phosphoproteome data from the two species are not very similar, the results reflect high similarity to the previously published dataset in terms of the pathways the phosphoproteins belong to. This study additionally provides evidence to prior observations that protein phosphorylation is common in bacteria. Notably, phosphoproteins identified in Pseudomonas aeruginosa belong to motility, transport, and pathogenicity pathways that are critical for survival and virulence. We report, for the first time, that motility regulator A, probably acting via the novel secondary messenger cyclic diguanylate monophosphate, significantly affects protein phosphorylation in Pseudomonas putida.

Original languageEnglish
Pages (from-to)2764-2775
Number of pages12
JournalProteomics
Volume9
Issue number10
DOIs
Publication statusPublished - 2009 May

Fingerprint

Phosphorylation
Pseudomonas
Bacteria
Phosphoproteins
Proteins
Eukaryota
Virulence
Pseudomonas putida
Critical Pathways
Protein-Serine-Threonine Kinases
Archaea
Threonine
Post Translational Protein Processing
Gram-Negative Bacteria
Pseudomonas aeruginosa
Serine
Tyrosine
Genes
Genome

Keywords

  • Cyclic diguanylate monophosphate
  • Metal oxide MS
  • Pathogenicity
  • Protein phosphorylation
  • Type VI secretion system

ASJC Scopus subject areas

  • Molecular Biology
  • Biochemistry

Cite this

Ser/Thr/Tyr phosphoproteome analysis of pathogenic and non-pathogenic Pseudomonas species. / Ravichandran, Ayshwarya; Sugiyama, Naoyuki; Tomita, Masaru; Swarup, Sanjay; Ishihama, Yasushi.

In: Proteomics, Vol. 9, No. 10, 05.2009, p. 2764-2775.

Research output: Contribution to journalArticle

Ravichandran, Ayshwarya ; Sugiyama, Naoyuki ; Tomita, Masaru ; Swarup, Sanjay ; Ishihama, Yasushi. / Ser/Thr/Tyr phosphoproteome analysis of pathogenic and non-pathogenic Pseudomonas species. In: Proteomics. 2009 ; Vol. 9, No. 10. pp. 2764-2775.
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