RibR, a possible regulator of theBacillus subtilisriboflavin biosynthetic operon,in vivointeracts with the 5â²-untranslated leader ofribmRNA
| Autor: | Yuhei Higashitsuji, Matthias Mack, Annemarie Angerer, Sabine Berghaus, Birgit Hobl |
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| Rok vydání: | 2007 |
| Předmět: |
Riboswitch
Operon Flavin group Bacillus subtilis Biology Microbiology chemistry.chemical_compound Bacterial Proteins Biosynthesis Flavins Two-Hybrid System Techniques Protein Interaction Mapping Genetics RNA Messenger Molecular Biology Gene Messenger RNA biology.organism_classification Yeast Phosphotransferases (Alcohol Group Acceptor) Biochemistry chemistry Mutation 5' Untranslated Regions |
| Zdroj: | FEMS Microbiology Letters. 274:48-54 |
| ISSN: | 1574-6968 0378-1097 |
| Popis: | RibR is a minor cryptic flavokinase (EC 2.7.1.26) of the Gram-positive bacterium Bacillus subtilis with an unknown cellular function. The flavokinase activity appears to be localized to the N-terminal domain of the protein. Using the yeast three-hybrid system, it was shown that RibR specifically interacts in vivo with the nontranslated wild-type leader of the mRNA of the riboflavin biosynthetic operon. This interaction is lost partially when a leader containing known cis-acting deregulatory mutations in the so-called RFN element is tested. The RFN element is a sequence within the rib-leader mRNA reported to serve as a receptor for an FMN-dependent 'riboswitch'. In RibR itself, interaction was localized to the carboxy-terminate part of the protein, a segment of unknown function that does not show similarity to other proteins in the public databases. Analysis of a ribR-defective strain revealed a mild deregulation with respect to flavin (riboflavin, FMN and FAD) biosynthesis. The results indicate that the RNA-binding protein RibR may be involved in the regulation of the rib genes. |
| Databáze: | OpenAIRE |
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