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The phosphorelay signal transduction pathway in the initiation of Bacillus subtilis sporulation
Author(s) -
Hoch James A.
Publication year - 1993
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.240510111
Subject(s) - bacillus subtilis , signal transduction , microbiology and biotechnology , biology , transduction (biophysics) , bacteria , biochemistry , genetics
The formation of spores in Bacillus subtilis is a developmental process under genetic control. The decision to either divide or sporulate is regulated by the state of phosphorylation of the Spo0A transcription factor. Phosphorylated Spo0A (Spo0A ∼ P) is both a repressor and an activator of transcription depending on the promoter it is affecting. Spo0A ∼ P is the end product of the phosphorelay, a signal transduction system linking environmental information to the activation of sporulation. Activation or deinhibition of two ATP‐dependent kinases, KinA and KinB, to phosphorylate the Spo0F secondary messenger initiates the phosphorelay. Spo0F ∼ P is the substrate for the Spo0B protein, a phosphoprotein phosphotransferase which transfers the phosphate group to Spo0A. The Spo0A ∼ P formed from this pathway orchestrates transcription events during the initial stage of spore development through direct effects on a variety of promoters and through the use of other transcription factors, termed transition state regulators, whose activity it controls. Because commitment to sporulation has serious cellular programming consequences and is not undertaken capriciously, the phosphorelay is subject to a variety of complex controls on the flow of phosphate through its components. © 1993 Wiley‐Liss, Inc.