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Article

Sequence diversity of apidaecin-like peptides arresting the terminating ribosome.

Nucleic acids research - 27 Aug 2024

Huang Weiping, Baliga Chetana, Vázquez-Laslop Nora, Mankin Alexander S

Abstract excerpt

The Proline-rich Antimicrobial Peptide (PrAMP) apidaecin (Api) inhibits translation by binding in the ribosomal nascent peptide exit tunnel, trapping release factors RF1 or RF2, and arresting ribosomes at stop codons. To explore the extent of sequence variations of the native 18-amino acid Api that allows it to preserve its activity, we screened a library of synthetic mutant Api genes expressed in bacterial...

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Share to Amino Acid Sequence
Share to Anti-Bacterial Agents
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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Codon, Terminator

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Share to Peptide Chain Termination, Translational

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Source

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Identifiers

PMID: 38953159
DOI: 10.1093/nar/gkae567
PMCID: PMC11347161

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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