Multiple histidine kinases regulate entry into stationary phase and sporulation in Bacillus subtilis

Authors

  • Min Jiang,

    1. Division of Cellular Biology, Department of Molecular and Experimental Medicine, MEM-116, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla,
      CA 92037, USA.
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  • Weilan Shao,

    1. Division of Cellular Biology, Department of Molecular and Experimental Medicine, MEM-116, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla,
      CA 92037, USA.
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  • Marta Perego,

    1. Division of Cellular Biology, Department of Molecular and Experimental Medicine, MEM-116, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla,
      CA 92037, USA.
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  • James A. Hoch

    Corresponding author
    • *For correspondence. E-mail hoch@scripps.edu; Tel. (+1) 858 784 7905; Fax (+1) 858 784 7966.

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Abstract

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.

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