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Nucleic Acids Research, 1994, Vol. 22, No. 13 2538-2546
© 1994

RNA

Structural elements of rpsO mRNA involved in the modulation of translational initiation and regulation of E.coli ribosomal protein S15

Claude Philippe, Lionel Bénard1, Flore Eyermann, Claire Cachia2, Stanislav V. Kirillov3, Claude Portier1, Bernard Ehresmann and Chantal Ehresmann*

UPR 9002 du CNRS, Institut de Biologie Moléculaire et Cellulaire 15 rue René Descartes, 67084-Strasbourg cedex 1Institut de Biologie Physico-Chimique 13 rue Pierre et Marie Curie, 75005-Paris 2Laboratoire de Biophysique, Faculté de Pharmacie 7 boulevard Jeanne d'Arc, 21000 Dijon, France 3Laboratory of Protein Biosynthesis, Nuclear Physic Institut 188350 Gatchina, St Petersbourg district, Russia

*To whom correspondence should be addressed

Received April 8, 1994. Revised May 31, 1994. Accepted May 31, 1994.

Previous experiments showed that S15 inhibits its own translation by binding to its mRNA in a region overlapping the ribosome loading site. This binding was postulated to stabilize a pseudoknot structure that exists in equilibrium with two stem-loops and to trap the ribosome on its mRNA loading site in a transitory state. In this study, we investigated the effect of mutations in the translational operator on: the binding of protein S15, the formation of the 30S/mRNA/tRNAMett ternary initiation complex, the ability of S15 to inhibit the formation of this ternary complex. The results were compared to in vivo expression and repression rates. The results show that (1) the pseudoknot is required for S15 recognition and translational control; (2) mRNA and 16S rRNA efficiently compete for S15 binding and 16S rRNA suppresses the ability of S15 to inhibit the formation of the active ternary complex; (3) the ribosome binds more efficiently to the pseudoknot than to the stem-loop; (4) sequences located between nucleotides 12 to 47 of the S15 coding phase enhances the efficiency of ribosome binding in vitro; this is correlated with enhanced in vivo expression and regulation rates.


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