MtrB from Bacillus subtilis binds specifically to trp leader RNA in a tryptophan-dependent manner.
- 1 January 1993
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 90 (1) , 128-132
- https://doi.org/10.1073/pnas.90.1.128
Abstract
MtrB regulates transcription attenuation of the Bacillus subtilis trp operon. We have shown that MtrB, either from B. subtilis or overexpressed in Escherichia coli, binds specifically to RNA from the leader region of the trp operon by a gel mobility-shift assay. This binding is tryptophan dependent. MtrB binds to a transcript terminated at the trp attenuator (-2 to +138) or a read-through transcript (-2 to +318). MtrB does not bind antisense trp leader RNA or single-stranded trp leader DNA. These results support the model in which attenuation is controlled by tryptophan-activated MtrB influencing the secondary structure of the leader region transcript to form a terminator structure.Keywords
This publication has 22 references indexed in Scilit:
- Reconstitution of Bacillus subtilis trp attenuation in vitro with TRAP, the trp RNA-binding attenuation protein.Proceedings of the National Academy of Sciences, 1993
- Conformation of the TAR RNA-Arginine Complex by NMR SpectroscopyScience, 1992
- cis-acting sites in the transcript of the Bacillus subtilis trp operon regulate expression of the operonJournal of Bacteriology, 1988
- RNA binding site of R17 coat proteinBiochemistry, 1987
- [1] Production of single-stranded plasmid DNAPublished by Elsevier ,1987
- Novel form of transcription attenuation regulates expression the Bacillus subtilis tryptophan operonJournal of Bacteriology, 1986
- A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes.Proceedings of the National Academy of Sciences, 1985
- Characterization of the Bacillus subtilis tryptophan promoter region.Proceedings of the National Academy of Sciences, 1984
- Stabilization of the hexameric form of Escherichia coli protein rho under ATP hydrolysis conditionsJournal of Molecular Biology, 1982
- A convenient computer program for fitting enzymatic rate laws to steady-state dataComputers and Biomedical Research, 1979