Activation of Bacillus subtilis Ugd by the BY-Kinase PtkA Proceeds via Phosphorylation of Its Residue Tyrosine 70

Dina Petranovic, C. Grangeasse, B. Macek, M. Abdillatef, V. Gueguen-Chaignon, S. Nessler, J. Deutscher, Ivan Mijakovic

    Research output: Contribution to journalJournal articleResearchpeer-review

    Abstract

    The phosphorylation-dependent activation of bacterial UDP-glucose dehydrogenases by BY-kinases has been previously described in several bacterial model organisms, but the identity of phosphorylated tyrosine(s) and the exact activation mechanism remained unknown. A recent site-specific phosphoproteomic study indicated that tyrosine 70 is phosphorylated in the Bacillus subtilis UDP-glucose dehydrogenase Ugd. In this study we confirm that this tyrosine 70 is indeed the main residue phosphorylated by the cognate BY-kinase PtkA. Homology-based modeling of the Ugd structure using structures from UDP-glucose/GDP-mannose dehydrogenases revealed that this residue is in close proximity to the NAD-binding site. We identified lysine 108 as the second important residue involved in Ugd activation. Enzymatic characterization of the Ugd proteins mutated in residues tyrosine 70 or lysine 108 suggested a phosphorylation-based regulatory mechanism. This study represents the first attempt to understand the activation of a bacterial enzyme by tyrosine phosphorylation at the molecular level.
    Original languageEnglish
    JournalJournal of Molecular Microbiology and Biotechnology
    Volume17
    Issue number2
    Pages (from-to)83-89
    ISSN1464-1801
    DOIs
    Publication statusPublished - 2009

    Keywords

    • Tyrosine phosphorylation
    • Enzyme activity
    • UDP-glucose dehydrogenase
    • Kinase

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