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

Mutations of highly conserved bases in the peptidyltransferase center induce compensatory rearrangements in yeast ribosomes.

RNA (New York, N.Y.) - 1 May 2011

Rakauskaite Rasa, Dinman Jonathan D

Abstract excerpt

Molecular dynamics simulation identified three highly conserved rRNA bases in the large subunit of the ribosome that form a three-dimensional (3D) "gate" that induces pausing of the aa-tRNA acceptor stem during accommodation into the A-site. A nearby fourth base contacting the "tryptophan finger" of yeast protein L3, which is involved in the coordinating elongation factor recruitment to the ribosome with...

Read the complete abstract on PubMed

Topics

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

Share to Base Sequence
Share to Nucleic Acid Conformation
Share to Peptidyl Transferases

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Protein Binding

Share to Protein Biosynthesis

Share to Ribosomes

Share to RNA, Ribosomal

Share to Saccharomyces cerevisiae

Source

Open in PubMed Open full text

Identifiers

PMID: 21441349
DOI: 10.1261/rna.2593211
PMCID: PMC3078735

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.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mutations of highly conserved bases in the peptidyltransferase center induce compensatory rearrangements in yeast ribosomes.PMID 21441349Read ↗

rRNA mutants in the yeast peptidyltransferase center reveal allosteric information networks and mechanisms of drug resistance.Semantic proximity Read ↗

Ribosomal protein L3 functions as a 'rocker switch' to aid in coordinating of large subunit-associated functions in eukaryotes and Archaea.Semantic proximity Read ↗

A molecular clamp ensures allosteric coordination of peptidyltransfer and ligand binding to the ribosomal A-site.Semantic proximity Read ↗

A flexible loop in yeast ribosomal protein L11 coordinates P-site tRNA binding.Semantic proximity Read ↗

An arc of unpaired "hinge bases" facilitates information exchange among functional centers of the ribosome.Semantic proximity Read ↗

Loss of Conserved rRNA Modifications in the Peptidyl Transferase Center Leads to Diminished Protein Synthesis and Cell Growth in Budding Yeast.Semantic proximity Read ↗

Mutational characterization and mapping of the 70S ribosome active site.Semantic proximity Read ↗

Crystal Structures of the uL3 Mutant Ribosome: Illustration of the Importance of Ribosomal Proteins for Translation Efficiency.Semantic proximity Read ↗

rRNA modifications in an intersubunit bridge of the ribosome strongly affect both ribosome biogenesis and activity.Semantic proximity Read ↗

Optimization of ribosome structure and function by rRNA base modification.Semantic proximity Read ↗

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

Ribosomal protein L3 mutants alter translational fidelity and promote rapid loss of the yeast killer virus.Semantic proximity Read ↗

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