Ontology highlight
ABSTRACT:
SUBMITTER: Mangano K
PROVIDER: S-EPMC7544508 | biostudies-literature | 2020 Oct
REPOSITORIES: biostudies-literature
eLife 20201008
Biochemical studies suggested that the antimicrobial peptide apidaecin (Api) inhibits protein synthesis by binding in the nascent peptide exit tunnel and trapping the release factor associated with a terminating ribosome. The mode of Api action in bacterial cells had remained unknown. Here genome-wide analysis reveals that in bacteria, Api arrests translating ribosomes at stop codons and causes pronounced queuing of the trailing ribosomes. By sequestering the available release factors, Api promo ...[more]