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Title: Systematic profiling of the bacterial phosphoproteome reveals bacterium-specific features of phosphorylation.
Authors: Lin, Miao-Hsia
Sugiyama, Naoyuki  kyouindb  KAKEN_id  orcid (unconfirmed)
Ishihama, Yasushi  kyouindb  KAKEN_id  orcid (unconfirmed)
Author's alias: 石濱, 泰
Issue Date: 15-Sep-2015
Publisher: American Association for the Advancement of Science
Journal title: Science signaling
Volume: 8
Issue: 394
Thesis number: rs10
Abstract: 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.
Rights: This is the author's version of the work. It is posted here by permission of the AAAS for personal use, not for redistribution. The definitive version was published in 'Science signaling' on 15 Sep 2015 DOI:10.1126/scisignal.aaa3117.
This is not the published version. Please cite only the published version.
DOI(Published Version): 10.1126/scisignal.aaa3117
PubMed ID: 26373674
Appears in Collections:Journal Articles

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