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  • Title: Characterization of Escherichia coli SecA protein binding to a site on its mRNA involved in autoregulation.
    Author: Dolan KM, Oliver DB.
    Journal: J Biol Chem; 1991 Dec 05; 266(34):23329-33. PubMed ID: 1720780.
    Abstract:
    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.
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