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Ribosomal protein S2 is an essential component of translation machinery, and its viable mutated variants conferring distinct phenotypes serve as a valuable tool in studying the role of S2 in translation regulation. One of a few availablerpsB mutants,rpsB1 , shows thermosensitivity and ensures enhanced expression of leaderless mRNAs. In this study, we identified the nature of therpsB1 mutation. Sequencing of therpsB1 allele revealed a G-to-A transition in the part of therpsB gene which encodes a coiled-coil domain of S2. The resulting E132K substitution resides in a highly conserved site, TKKE, a so-called N-terminal capping box, at the beginning of the second alpha helix. The protruding coiled-coil domain of S2 is known to provide binding with 16S rRNA in the head of the 30S subunit and, in addition, to interact with a key mRNA binding protein, S1. Molecular dynamics simulations revealed a detrimental impact of the E132K mutation on the coiled-coil structure and thereby on the interactions between S2 and 16S rRNA, providing a clue for the thermosensitivity of therpsB1 mutant. Using a strain producing a leaderlesslacZ transcript from the chromosomallac promoter, we demonstrated that not only therpsB1 mutation generating S2/S1-deficient ribosomes but also therpsA ::IS10 mutation leading to partial deficiency in S1 alone increased translation efficiency of the leaderless mRNA by about 10-fold. Moderate overexpression of S1 relieved all these effects and, moreover, suppressed the thermosensitive phenotype ofrpsB1 , indicating the role of S1 as an extragenic suppressor of the E132K mutation.

journal of bacteriology

A Single Missense Mutation in a Coiled-Coil Domain of Escherichia coli Ribosomal Protein S2 Confers a Thermosensitive Phenotype That Can Be Suppressed by Ribosomal Protein S1