Bacterial
ribosomes stalled on defective messenger RNAs (mRNAs) are rescued by tmRNA, an ∼ 300 - nucleotide - long molecule that functions as both transfer RNA (tRNA) and mRNA.
Expression of the Escherichia coli tryptophanase operon depends on
ribosome stalling during translation of the upstream TnaC leader peptide, a process for which interactions between the TnaC nascent chain and the ribosomal exit tunnel are critical.
We determined a 5.8 angstrom — resolution cryo — electron microscopy and single - particle reconstruction of
a ribosome stalled during translation of the tnaC leader gene.
Not exact matches
Proteins are produced by
ribosomes, and misfolding can occur if they
stall while decoding a damaged template.
Too much structure could force the
ribosome to do extra work untangling the strand or even
stall translation altogether.
One of the defects is an error in mouse t - RNA (another type of RNA involved in translation) that
stalls the
ribosome and the other is a defect in the system that rescues the
ribosome when it
stalls.
When the drug is present, it binds within the tunnel of the
ribosome and interacts with the translating leader peptide to
stall protein synthesis.
Using cryo - electron microscopy to study the structure of such
ribosome - mRNA complexes, the researchers were able to show the manner in which special rescue proteins (Dom34 and Hbs1) recognize such
stalled ribosomes, thereby initiating the splitting of the arrested complex and the degradation of the faulty mRNA.