A role for Asp75 in domain interactions in the Bacillus subtilis response regulator Spo0A
| Autor: | George B. Spiegelman, Marguerite A. Cervin |
|---|---|
| Rok vydání: | 2000 |
| Předmět: |
Protein Conformation
Mutant Bacillus subtilis Biochemistry Bacterial Proteins Transcription (biology) Phosphorylation Molecular Biology Polymerase chemistry.chemical_classification Spores Bacterial biology Activator (genetics) fungi Wild type Cell Biology biology.organism_classification Amino acid Response regulator chemistry biology.protein bacteria Asparagine Transcription Factors |
| Zdroj: | The Journal of biological chemistry. 275(29) |
| ISSN: | 0021-9258 |
| Popis: | Spo0A is a two-domain response regulator required for sporulation initiation in Bacillus subtilis. Studies on response regulators have focused on the activity of each domain, but very little is known about the mechanism by which the regulatory domain inhibits the activator domain. In this study, we created a single amino acid substitution in the regulatory domain, D75S, which resulted in a dramatic decrease in sporulation in vivo. In vitro studies with the purified Spo0AD75S protein demonstrated that phosphorylation and DNA binding were comparable with wild type Spo0A. However, the mutant was unable to stimulate transcription by final sigma(A)-RNA polymerase from the Spo0A-dependent spoIIG operon promoter. We suggest that the amino acid Asp(75) and/or the region within which it resides, the alpha3-beta4 loop, are involved in the inhibitory interaction between the regulatory and activator domains of Spo0A. |
| Databáze: | OpenAIRE |
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