Systematic profiling of the bacterial phosphoproteome reveals bacterium-specific features of phosphorylation.

• Lin, Miao-Hsia

• Sugiyama, Naoyuki

• 石濱, 泰

抄録

Protein phosphorylation is a crucial posttranslational modification for regulating cellular processes in bacteria; however, it has not been extensively studied because of technical difficulties in the enrichment of phosphopeptides. We devised an enrichment protocol that enabled the identification of >1000 phosphopeptides from a single bacterial sample. We discovered three high-confidence serine and threonine phosphorylation motifs, as well as 29 other motifs at various levels of confidence, from three distinct bacterial phosphoproteomes. We found that the proline-directed and basophilic phosphorylation motifs that are commonly enriched in eukaryotes were not observed in bacteria. Unlike eukaryotes, bacteria had a low occurrence of both phosphorylation and acetylation in N-terminal phosphopeptides. Because infection of host cells by bacterial pathogens is often accompanied by kinase-mediated phosphorylation events, the differences in phosphorylation preferences between bacteria and eukaryotes revealed by this study could be useful in identifying bacterial-specific targets for future therapies.

収録刊行物

• Science signaling

  Science signaling 8 (394), 2015-09-15

  American Association for the Advancement of Science

詳細情報

• CRID: 1050001335818858752
• NII論文ID: 120005682544
• ISSN: 19379145
• HANDLE: 2433/202909
• 本文言語コード: en
• 資料種別: journal article
• データソース種別:
  • IRDB
  • CiNii Articles