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Subunit composition and domain structure of the Spo0A sporulation transcription factor of Bacillus subtilis.
- Source :
-
The Journal of biological chemistry [J Biol Chem] 1994 Jun 17; Vol. 269 (24), pp. 16977-82. - Publication Year :
- 1994
-
Abstract
- The Spo0A transcription factor is responsible for the initiation of sporulation and is active in transcription only after phosphorylation by a specific signal transduction pathway, the phosphorelay. The effect of phosphorylation on the physical properties of Spo0A was determined. Spo0A and Spo0A approximately P both behaved as monomers during Sephacryl chromatography and gel electrophoresis, suggesting that phosphorylation did not modify the oligomerization state of the protein. Trypsin digested Spo0A at a single cleavage site between residues 142 and 143 within a hinge connecting two tightly folded domains. The amino domain retains ability to be phosphorylated by the phosphorelay. The carboxyl domain is active as a DNA-binding protein and retains the sequence specificity of the intact molecule for 0A boxes on the abrB promoter as revealed by footprinting studies. The carboxyl domain stimulated in vitro transcription from the spoIIG promoter 5-fold greater than an equal amount of Spo0A and about half as well as equivalent amounts of Spo0A approximately P. Thus, the unphosphorylated amino domain inhibits the transcription stimulation activity of the carboxyl domain. We suggest that phosphorylation activates transcription regulation functions of Spo0A by modifying the spatial relationships of the amino and carboxyl domains.
- Subjects :
- Bacterial Proteins isolation & purification
Base Sequence
Binding Sites
Chromatography, Affinity
Chromatography, Gel
Cloning, Molecular
Electrophoresis, Polyacrylamide Gel
Escherichia coli
Genes, Bacterial
Kinetics
Macromolecular Substances
Molecular Sequence Data
Molecular Weight
Oligodeoxyribonucleotides metabolism
Peptide Fragments chemistry
Peptide Fragments isolation & purification
Peptide Mapping
Phosphorylation
Protein Folding
Recombinant Proteins chemistry
Recombinant Proteins isolation & purification
Recombinant Proteins metabolism
Transcription Factors isolation & purification
Bacillus subtilis metabolism
Bacterial Proteins chemistry
Bacterial Proteins metabolism
Promoter Regions, Genetic
Transcription Factors chemistry
Transcription Factors metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0021-9258
- Volume :
- 269
- Issue :
- 24
- Database :
- MEDLINE
- Journal :
- The Journal of biological chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 8207022