Abstract:
:The Spo0A protein of Bacillus subtilis is 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 the spo0F promoter region, and stimulates the transcription from the P2 promoter recognized by sigma H-RNA polymerase. Biochemical and biological analyses suggest that phospho-Spo0A interacts directly with the "0A-like box" sequence (TGTCGTA) located in the spo0F promoter region. Phosphorylation of Spo0A enhanced its affinity to the 0A-like box. Evidence is also presented that the spo0F promoter 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.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Asayama M,Yamamoto A,Kobayashi Ydoi
10.1006/jmbi.1995.0354subject
Has Abstractpub_date
1995-06-30 00:00:00pages
11-23issue
1eissn
0022-2836issn
1089-8638pii
S0022-2836(85)70354-3journal_volume
250pub_type
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