Abstract
The Spo0A protein ofBacillus subtilisis a transcriptional regulator that shows extensive homology to the regulator proteins in bacterial two-component regulatory systems. Phosphorylation of Spo0A is absolutely necessary for the initiation of sporulation. We now show that phospho-Spo0A is a dimer, binds specifically to thespo0Fpromoter region, and stimulates the transcription from the P2 promoter recognized by σH-RNA polymerase. Biochemical and biological analyses suggest that phospho-Spo0A interacts directly with the “0A-like box” sequence (TGTCGTA) located in thespo0Fpromoter region. Phosphorylation of Spo0A enhanced its affinity to the 0A-like box. Evidence is also presented that thespo0Fpromoter region contains a static bend having two sets of oligo(dA-dT) tracts. It was demonstrated that the bending region overlaps with the recognition site for the phospho-Spo0A.f2f2Present address: M. Asayama, Faculty of Agriculture, Ibaraki University, Ami, Ibaraki 300-03, Japan.
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