What question did this study set out to answer?

Characterize the global Ser/Thr phosphoproteome of Mycobacterium tuberculosis and determine the substrate sequence specificity across its 11 serine/threonine protein kinases.

April 5, 2010Proceedings of the National Academy of SciencesOpen Access

Extensive phosphorylation with overlapping specificity by Mycobacterium tuberculosis serine/threonine protein kinases

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Authors

SPSladjana PrišićUniversity of Hawaiʻi at Mānoa SDSelasi DankwaInfectious Disease Research Institute DSDaniel SchwartzWestchester Medical Center

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Implication

Phosphoproteomic profiling reveals extensive phosphorylation across 301 proteins in Mycobacterium tuberculosis, highlighting shared substrate motifs among serine/threonine kinases.

Key Points

Characterize the global Ser/Thr phosphoproteome of Mycobacterium tuberculosis and determine the substrate sequence specificity across its 11 serine/threonine protein kinases.
Conducted a phosphoproteomic survey in Mycobacterium tuberculosis to map global protein phosphorylation sites.
Performed quantitative in vitro kinase assays and bioinformatic motif analyses on peptide arrays containing identified phosphorylation sequences.
Tested substrate recognition using peptide libraries with systematic amino acid substitutions surrounding the phosphoacceptor residue.
Identified more than 500 phosphorylation events spanning 301 distinct proteins associated with diverse physiological pathways.
Determined that six of the 11 serine/threonine protein kinases share a single dominant phosphorylation consensus motif.
Demonstrated that peripheral amino acid substitutions establish distinct sub-preferences for individual kinases, enabling cognate kinase predictions for candidate phosphoproteins.

Cite This Study

Prišić et al. (2010) studied this question.

synapsesocial.com/papers/6aa9eee4dbbe4230954814da https://doi.org/10.1073/pnas.0913482107

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Implication

Phosphoproteomic profiling reveals extensive phosphorylation across 301 proteins in Mycobacterium tuberculosis, highlighting shared substrate motifs among serine/threonine kinases.

Extensive phosphorylation with overlapping specificity by Mycobacterium tuberculosis serine/threonine protein kinases

Discussion

Member takes

Implication

Key Points

Cite This Study

Extensive phosphorylation with overlapping specificity by Mycobacterium tuberculosis serine/threonine protein kinases

Discussion

Member takes

Implication

Key Points

Cite This Study

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