Interactions of the TnaC nascent peptide with rRNA in the exit tunnel enable the ribosome to respond to free tryptophan. Academic Article uri icon

abstract

  • A transcriptional attenuation mechanism regulates expression of the bacterial tnaCAB operon. This mechanism requires ribosomal arrest induced by the regulatory nascent TnaC peptide in response to free L-tryptophan (L-Trp). In this study we demonstrate, using genetic and biochemical analyses, that in Escherichia coli, TnaC residue I19 and 23S rRNA nucleotide A2058 are essential for the ribosome's ability to sense free L-Trp. We show that the mutational change A2058U in 23S rRNA reduces the concentration dependence of L-Trp-mediated tna operon induction, whereas the TnaC I19L change suppresses this phenotype, restoring the sensitivity of the translating A2058U mutant ribosome to free L-Trp. These findings suggest that interactions between TnaC residue I19 and 23S rRNA nucleotide A2058 contribute to the creation of a regulatory L-Trp binding site within the translating ribosome.

published proceedings

  • Nucleic Acids Res

altmetric score

  • 0.5

author list (cited authors)

  • Martnez, A. K., Gordon, E., Sengupta, A., Shirole, N., Klepacki, D., Martinez-Garriga, B., ... Cruz-Vera, L. R.

citation count

  • 29

complete list of authors

  • Martínez, Allyson K||Gordon, Emily||Sengupta, Arnab||Shirole, Nitin||Klepacki, Dorota||Martinez-Garriga, Blanca||Brown, Lewis M||Benedik, Michael J||Yanofsky, Charles||Mankin, Alexander S||Vazquez-Laslop, Nora||Sachs, Matthew S||Cruz-Vera, Luis R

publication date

  • January 2014