Enabling stop codon read-through translation in bacteria as a probe for amyloid aggregation.

ABSTRACT: Amyloid aggregation of the eukaryotic translation terminator eRF3/Sup35p, the [PSI ⁺] prion, empowers yeast ribosomes to read-through UGA stop codons. No similar functional prion, skipping a stop codon, has been found in Escherichia coli, a fact possibly due to the efficient back-up systems found in bacteria to rescue non-stop complexes. Here we report that engineering hydrophobic amyloidogenic repeats from a synthetic bacterial prion-like protein (RepA-WH1) into the E. coli releasing factor RF1 promotes its aggregation and enables ribosomes to continue with translation through a premature UAG stop codon located in a β-galactosidase reporter. To our knowledge, intended aggregation of a termination factor is a way to overcome the bacterial translation quality checkpoint that had

SUBMITTER: Molina-Garcia L 

PROVIDER: S-EPMC5605706 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature