Phosphoproteomics analysis of a clinical mycobacterium tuberculosis Beijing isolate : expanding the mycobacterial phosphoproteome catalog

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dc.contributor.authorFortuin, Sueretaen_ZA
dc.contributor.authorTomazella, Gisele G.en_ZA
dc.contributor.authorNagaraj, Nagarjunaen_ZA
dc.contributor.authorSampson, Samantha L.en_ZA
dc.contributor.authorGey Van Pittius, Nicolaas C.en_ZA
dc.contributor.authorSoares, Nelson C.en_ZA
dc.contributor.authorWiker, Harald G.en_ZA
dc.contributor.authorDe Souza, Gustavo A.en_ZA
dc.contributor.authorWarren, Robin M.en_ZA
dc.date.accessioned2016-11-14T10:41:56Z
dc.date.available2016-11-14T10:41:56Z
dc.date.issued2015
dc.descriptionCITATION: Fortuin, S., et al. 2015. Phosphoproteomics analysis of a clinical mycobacterium tuberculosis beijing isolate : expanding the mycobacterial phosphoproteome catalog. Frontiers in Microbiology, 6:6, doi:10.3389/fmicb.2015.00006.
dc.descriptionThe original publication is available at www.frontiersin.org
dc.description.abstractReversible protein phosphorylation, regulated by protein kinases and phosphatases, mediates a switch between protein activity and cellular pathways that contribute to a large number of cellular processes. The Mycobacterium tuberculosis genome encodes 11 Serine/Threonine kinases (STPKs) which show close homology to eukaryotic kinases. This study aimed to elucidate the phosphoproteomic landscape of a clinical isolate of M. tuberculosis. We performed a high throughput mass spectrometric analysis of proteins extracted from an early-logarithmic phase culture. Whole cell lysate proteins were processed using the filter-aided sample preparation method, followed by phosphopeptide enrichment of tryptic peptides by strong cation exchange (SCX) and Titanium dioxide (TiO2) chromatography. The MaxQuant quantitative proteomics software package was used for protein identification. Our analysis identified 414 serine/threonine/tyrosine phosphorylated sites, with a distribution of S/T/Y sites; 38% on serine, 59% on threonine and 3% on tyrosine; present on 303 unique peptides mapping to 214 M. tuberculosis proteins. Only 45 of the S/T/Y phosphorylated proteins identified in our study had been previously described in the laboratory strain H37Rv, confirming previous reports. The remaining 169 phosphorylated proteins were newly identified in this clinical M. tuberculosis Beijing strain. We identified 5 novel tyrosine phosphorylated proteins. These findings not only expand upon our current understanding of the protein phosphorylation network in clinical M. tuberculosis but the data set also further extends and complements previous knowledge regarding phosphorylated peptides and phosphorylation sites in M. tuberculosis.en_ZA
dc.description.urihttp://journal.frontiersin.org/article/10.3389/fmicb.2015.00006/full
dc.description.versionPublisher's version
dc.format.extent12 pages
dc.identifier.citationFortuin, S., et al. 2015. Phosphoproteomics analysis of a clinical mycobacterium tuberculosis beijing isolate : expanding the mycobacterial phosphoproteome catalog. Frontiers in Microbiology, 6:6, doi:10.3389/fmicb.2015.00006
dc.identifier.issn1664-302X (online)
dc.identifier.otherdoi:10.3389/fmicb.2015.00006
dc.identifier.urihttp://hdl.handle.net/10019.1/99846
dc.language.isoen_ZAen_ZA
dc.publisherFrontiers Media
dc.rights.holderAuthors retain copyright
dc.subjectMycobacterium tuberculosis -- Microbiologyen_ZA
dc.subjectTyrosine phosphorylationen_ZA
dc.subjectTyrosine protein kinaseen_ZA
dc.subjectPhosphopreteomicsen_ZA
dc.titlePhosphoproteomics analysis of a clinical mycobacterium tuberculosis Beijing isolate : expanding the mycobacterial phosphoproteome catalogen_ZA
dc.typeArticleen_ZA
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