Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Stop codon recognition by release factors induces structural rearrangement of the ribosomal decoding center that is productive for peptide release.

Molecular cell - 30 Nov 2007

Youngman Elaine M, He Shan L, Nikstad Laura J, Green Rachel

Abstract excerpt

Peptide release on the ribosome is catalyzed in the large subunit peptidyl transferase center by release factors on recognition of stop codons in the small subunit decoding center. Here we examine the role of the decoding center in this process. Mutation of decoding center nucleotides or removal of 2'OH groups from the codon--deleterious in the related process of tRNA selection--has only mild effects on peptide...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Aminoglycosides
Share to Anti-Bacterial Agents

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Codon, Terminator

Share to Deoxyribonucleotides

Share to Peptide Termination Factors

Share to Peptides

Share to Ribosomes

Share to Structure-Activity Relationship

Source

Identifiers

PMID: 18042450
DOI: 10.1016/j.molcel.2007.09.015

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Stop codon recognition by release factors induces structural rearrangement of the ribosomal decoding center that is productive for peptide release.PMID 18042450Read ↗

A model for how ribosomal release factors induce peptidyl-tRNA cleavage in termination of protein synthesis.Semantic proximity Read ↗

Peptide release on the ribosome: mechanism and implications for translational control.Semantic proximity Read ↗

Two distinct conformations of the conserved RNA-rich decoding center of the small ribosomal subunit are recognized by tRNAs and release factors.Semantic proximity Read ↗

Various effects of paromomycin on tmRNA-directed trans-translation.Semantic proximity Read ↗

Mutational analysis of S12 protein and implications for the accuracy of decoding by the ribosome.Semantic proximity Read ↗

Mapping functionally important motifs SPF and GGQ of the decoding release factor RF2 to the Escherichia coli ribosome by hydroxyl radical footprinting. Implications for macromolecular mimicry and structural changes in RF2.Semantic proximity Read ↗

Polypeptide release at sense and noncognate stop codons by localized charge-exchange alterations in translational release factors.Semantic proximity Read ↗

Mutations at the accommodation gate of the ribosome impair RF2-dependent translation termination.Semantic proximity Read ↗

The critical role of the universally conserved A2602 of 23S ribosomal RNA in the release of the nascent peptide during translation termination.Semantic proximity Read ↗

Structural basis for the context-specific action of classic peptidyl transferase inhibitorsSemantic proximity Read ↗

The ribosomal binding and peptidyl-tRNA hydrolysis functions of Escherichia coli release factor 2 are linked through residue 246.Semantic proximity Read ↗

Ribosomal release without peptidyl tRNA hydrolysis at translation termination in a eukaryotic system.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.