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Molecular basis for the ribosome functioning as an L-tryptophan sensor.

Abstract：

:Elevated levels of the free amino acid L-tryptophan (L-Trp) trigger expression of the tryptophanase tnaCAB operon in E. coli. Activation depends on tryptophan-dependent ribosomal stalling during translation of the upstream TnaC peptide. Here, we present a cryoelectron microscopy (cryo-EM) reconstruction at 3.8 Å resolution of a ribosome stalled by the TnaC peptide. Unexpectedly, we observe two L-Trp molecules in the ribosomal exit tunnel coordinated within composite hydrophobic pockets formed by the nascent TnaC peptide and the tunnel wall. As a result, the peptidyl transferase center (PTC) adopts a distinct conformation that precludes productive accommodation of release factor 2 (RF2), thereby inducing translational stalling. Collectively, our results demonstrate how the translating ribosome can act as a small molecule sensor for gene regulation.

journal_name

Cell Rep

journal_title

Cell reports

authors

Bischoff L,Berninghausen O,Beckmann R

doi

10.1016/j.celrep.2014.09.011

subject

Has Abstract

pub_date

2014-10-23 00:00:00

pages

469-75

issue

2

issn

2211-1247

pii

S2211-1247(14)00779-7

journal_volume

9

pub_type

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