Characterization of a membrane-linked Ser/Thr protein kinase in Bacillus subtilis, implicated in developmental processes.

摘要: PrkC was shown to be a eukaryotic-like (Hanks-type) protein kinase from Bacillus subtilis with structural organization similar that of the eukaryotic sensor Ser/Thr or Tyr kinases (e.g. TGF beta PDGF receptors). The molecule consists catalytic domain located in cytoplasm, joined by single transmembrane-spanning region (TMD) large extracellular domain. Using genetic reporter system, involving cI repressor lambda, evidence obtained indicating forms dimer, both TMD and external dimerization. purified autophosphorylate phosphorylate an target, MBP, cases on threonine. These two functions require completely conserved K40 residue subdomain II, which is essential for enzymatic activity. Importantly, mutant deleted prkC K40R exhibit decreased efficiency sporulation significant reduction biofilm formation, demonstrating activity necessary these developmental processes. In addition, we showed product prpC, PPM phosphatase encoded adjacent gene, co-transcribed prkC, also required normal spore formation.