Abstract
In prokaryotes, protein-mediated translational control often takes the form of a negative feedback (Gold, 1988; Lindahl et al., 1986). The translational repressor, as proven in some examples, interacts with a regulatory region of its own mRNA, affecting ribosome binding and thus translation. In some cases in bacteriophage and E.coli, a particular feedback was shown to belong to a more general regulatory system. For instance, a particular feedback due to a specific ribosomal regulatory protein is modulated by the cellular concentration of the ribosomal RNA (rRNA) to which it binds (Nomura et al., 1984). If the cellular rRNA concentration increases, the specific regulatory protein binds to the excess of rRNA and not to its own mRNA whose translation is increased. This mRNA-rRNA competition permits the ribosomal protein synthesis to be adapted to the cellular rRNA concentration. As suggested in several cases, the binding site of the ribosomal regulatory protein on both its ligands (mRNA and rRNA) could share some similarity. This hypothesis has been called molecular mimicry (Campbell et al, 1983) and implies that there is a common site on the regulatory protein that recognises both nucleic acid ligands. This is a simple strategy for adding a regulatory role to a protein involved in nucleic acid binding without having the necessity for a separate regulatory domain.
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Springer, M. et al. (1990). Translational Feedback Control in E.Coli: The Role of tRNAThr and tRNAThr-Like Structures in the Operator of the Gene for Threonyl-tRNA Synthetase. In: McCarthy, J.E.G., Tuite, M.F. (eds) Post-Transcriptional Control of Gene Expression. NATO ASI Series, vol 49. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-75139-4_29
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DOI: https://doi.org/10.1007/978-3-642-75139-4_29
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