ArticleRNA (New York, N.Y.)2015
Activities of the peptidyl transferase center of ribosomes lacking protein L27.
Article in RNA (New York, N.Y.), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 23 citations in OpenAlex.
- 23S rRNA modifications stimulate catalytic activity and prevent the formation of alternative structures.Nucleic acids research · 2026Article
- Ribosomal protein bL27 protects translating ribosomes from tmRNA-SmpB.Science advances · 2026Article
- Ribosomal Protein bL27 Protects Translating Ribosomes from tmRNA-SmpB.bioRxiv : the preprint server for biology · 2026Article
- Cleavage ofbioRxiv : the preprint server for biology · 2025Article
- Phage-Related Ribosomal Proteases (Prps): Discovery, Bioinformatics, and Structural Analysis.Antibiotics (Basel, Switzerland) · 2022Article
- A switch from α-helical to β-strand conformation during co-translational protein folding.The EMBO journal · 2022Article
- The Peptidyl Transferase Center: a Window to the Past.Microbiology and molecular biology reviews : MMBR · 2021Article
- Translation in Prokaryotes.Cold Spring Harbor perspectives in biology · 2018Review
- Morphological Observation and Comparative Transcriptomic Analysis of Clostridium perfringens Biofilm and Planktonic Cells.Current microbiology · 2018Article
- Mechanistic alternatives for peptide bond formation on the ribosome.Nucleic acids research · 2018Article
- Regulation of Ribosomal Protein Operons rplM-rpsI, rpmB-rpmG, and rplU-rpmA at the Transcriptional and Translational Levels.Journal of bacteriology · 2016Article
- A combined cryo-EM and molecular dynamics approach reveals the mechanism of ErmBL-mediated translation arrest.Nature communications · 2016Article
- Structural Basis for Translation Termination on a Pseudouridylated Stop Codon.Journal of molecular biology · 2016Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The ribosome is the molecular machine responsible for protein synthesis in all living organisms. Its catalytic core, the peptidyl transferase center (PTC), is built of rRNA, although several proteins reach close to the inner rRNA shell. In the Escherichia coli ribosome, the flexible N-terminal tail of the ribosomal protein L27 contacts the A- and P-site tRNA. Based on computer simulations of the PTC and on previous biochemical evidence, the N-terminal α-amino group of L27 was suggested to take part in the peptidyl-transfer reaction. However, the contribution of this group to catalysis has not been tested experimentally. Here we investigate the role of L27 in peptide-bond formation using fast kinetics approaches. We show that the rate of peptide-bond formation at physiological pH, both with aminoacyl-tRNA or with the substrate analog puromycin, is independent of the presence of L27; furthermore, translation of natural mRNAs is only marginally affected in the absence of L27. The pH dependence of the puromycin reaction is unaltered in the absence of L27, indicating that the N-terminal α-amine is not the ionizing group taking part in catalysis. Likewise, L27 is not required for the peptidyl-tRNA hydrolysis during termination. Thus, apart from the known effect on subunit association, which most likely explains the phenotype of the deletion strains, L27 does not appear to be a key player in the core mechanism of peptide-bond formation on the ribosome.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.