2015年9月
Systematic profiling of the bacterial phosphoproteome reveals bacterium- specific features of phosphorylation
SCIENCE SIGNALING
- ,
- ,
- 巻
- 8
- 号
- 394
- 開始ページ
- rs10
- 終了ページ
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1126/scisignal.aaa3117
- 出版者・発行元
- AMER ASSOC ADVANCEMENT SCIENCE
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.
- リンク情報
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- DOI
- https://doi.org/10.1126/scisignal.aaa3117
- PubMed
- https://www.ncbi.nlm.nih.gov/pubmed/26373674
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000363317200004&DestApp=WOS_CPL
- URL
- http://orcid.org/0000-0001-7633-8495
- ID情報
-
- DOI : 10.1126/scisignal.aaa3117
- ISSN : 1945-0877
- eISSN : 1937-9145
- ORCIDのPut Code : 58378556
- PubMed ID : 26373674
- Web of Science ID : WOS:000363317200004