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Multiple histidine kinases regulate entry into stationary phase and sporulation in Bacillus subtilis
Author(s) -
Jiang Min,
Shao Weilan,
Perego Marta,
Hoch James A.
Publication year - 2000
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1046/j.1365-2958.2000.02148.x
Subject(s) - bacillus subtilis , kinase , biology , response regulator , histidine kinase , protein serine threonine kinases , phosphorylation , biochemistry , microbiology and biotechnology , transcription (linguistics) , histidine , bacteria , protein kinase a , gene , genetics , enzyme , bacterial protein , linguistics , philosophy
Protein homology studies identified five kinases potentially capable of phosphorylating the Spo0F response regulator and initiating sporulation in Bacillus subtilis . Two of these kinases, KinA and KinB, were known from previous studies to be responsible for sporulation in laboratory media. In vivo studies of the activity of four of the kinases, KinA, KinC, KinD ( ykvD ) and KinE ( ykrQ ), using abrB transcription as an indicator of Spo0A∼P level, revealed that KinC and KinD were responsible for Spo0A∼P production during the exponential phase of growth in the absence of KinA and KinB. In vitro , all four kinases dephosphorylated Spo0F∼P with the production of ATP at approximately the same rate, indicating that they possess approximately equal affinity for Spo0F. All the kinases were expressed during growth and early stationary phase, suggesting that the differential activity observed in growth and sporulation results from differential activation by signal ligands unique to each kinase.