Deletion of the RluD pseudouridine synthase promotes SsrA peptide tagging of ribosomal protein S7

摘要: Summary RluD catalyses formation of three pseudouridine residues within helix 69 the 50S ribosome subunit. Helix makes important contacts with decoding centre on 30S subunit and deletion rluD was recently shown to interfere translation termination in Escherichia coli. Here, we show that increases tmRNA activity ribosomes undergoing release factor 2 (RF2)-mediated at UGA stop codons. Strikingly, tmRNA-mediated SsrA peptide tagging two proteins, ribosomal protein S7 LacI, dramatically increased ΔrluD cells. due a unique C-terminal extension found E. coli K-12 strains. Introduction rpsG gene (encoding S7) from an B strain abrogated background, partially complemented mutant's slow-growth phenotype. Additionally, exchange prfB RF2) allele greatly reduced In contrast cells, resulted no growth These findings indicate originally observed phenotypes result synthetic interactions alleles