Characterization of Escherichia coli SecA protein binding to a site on its mRNA involved in autoregulation.
In order to understand further the autogenous regulation of Escherichia coli secA translation, we have set up a purified system to study the binding of SecA protein to portions of its mRNA. Specific SecA protein-RNA binding was demonstrated by UV cross-linking, filter binding, and gel shift assays. Use of the filter binding assay allowed optimization of binding, which was influenced by Mg2+ and ATP concentrations, and a measurement of the affinity of this interaction. A nested series of RNAs lacking either 5' or 3' portions of geneX-secA sequences were used to localize the SecA protein binding site to sequences around the geneX-secA intergenic region. These studies imply that SecA protein directly regulates its own translation by a specific RNA binding activity that presumably blocks translational initiation.[1]References
- Characterization of Escherichia coli SecA protein binding to a site on its mRNA involved in autoregulation. Dolan, K.M., Oliver, D.B. J. Biol. Chem. (1991) [Pubmed]
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