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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Transmembrane modulator-dependent bacterial tyrosine kinase activates UDP-glucose dehydrogenases.

Protein-tyrosine kinases regulating bacterial exopolysaccharide synthesis autophosphorylate on tyrosines located in a conserved C-terminal region. So far no other substrates have been identified for these kinases. Here we demonstrate that Bacillus subtilis YwqD not only autophosphorylates at Tyr-228, but that it also phosphorylates the two UDP-glucose dehydrogenases (UDP-glucose DHs) YwqF and TuaD at a tyrosine residue. However, phosphorylation of YwqF and TuaD occurs only in the presence of the transmembrane protein YwqC. The presumed intracellular C-terminal part of YwqC (last 50 amino acids) seems to interact with the tyrosine-kinase and to allow YwqD-catalysed phosphorylation of the two UDP-glucose DHs, which are key enzymes for the synthesis of acidic polysaccharides. However, only when phosphorylated by YwqD do the two enzymes exhibit detectable UDP-glucose DH activity. Dephosphorylation of P-Tyr-YwqF and P-Tyr-TuaD by the P-Tyr-protein phosphatase YwqE switched off their UDP-glucose DH activity. YwqE, which is encoded by the fourth gene of the B.subtilis ywqCDEF operon, also dephosphorylates P-Tyr-YwqD.[1]

References

  1. Transmembrane modulator-dependent bacterial tyrosine kinase activates UDP-glucose dehydrogenases. Mijakovic, I., Poncet, S., Boël, G., Mazé, A., Gillet, S., Jamet, E., Decottignies, P., Grangeasse, C., Doublet, P., Le Maréchal, P., Deutscher, J. EMBO J. (2003) [Pubmed]
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