ArticleThe EMBO journal2011
The 2'-OH group of the peptidyl-tRNA stabilizes an active conformation of the ribosomal PTC.
Article in The EMBO journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 59 citations in OpenAlex.
- Mechanism of release factor-mediated peptidyl-tRNA hydrolysis on the ribosome.Science (New York, N.Y.) · 2025Article
- 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
- Decoding on the ribosome depends on the structure of the mRNA phosphodiester backbone.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Translational roles of the C75 2'OH in an in vitro tRNA transcript at the ribosomal A, P and E sites.Scientific reports · 2017Article
- Induced fit of the peptidyl-transferase center of the ribosome and conformational freedom of the esterified amino acids.RNA (New York, N.Y.) · 2017Article
- Article
- A combined cryo-EM and molecular dynamics approach reveals the mechanism of ErmBL-mediated translation arrest.Nature communications · 2016Article
- Nascent peptide assists the ribosome in recognizing chemically distinct small molecules.Nature chemical biology · 2016Article
- Activities of the peptidyl transferase center of ribosomes lacking protein L27.RNA (New York, N.Y.) · 2015Article
- Peptide Bond Formation Mechanism Catalyzed by Ribosome.Journal of the American Chemical Society · 2015Article
- Protein Synthesis with Ribosomes Selected for the Incorporation of β-Amino Acids.Biochemistry · 2015Article
- The juxtaposition of ribose hydroxyl groups: the root of biological catalysis and the RNA world?Origins of life and evolution of the biosphere : the journal of the International Society for the Study of the Origin of Life · 2015Article
- The ribosome can discriminate the chirality of amino acids within its peptidyl-transferase center.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- A proton wire to couple aminoacyl-tRNA accommodation and peptide-bond formation on the ribosome.Nature structural & molecular biology · 2014Article
- Speciation of a group I intron into a lariat capping ribozyme.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Slicing tRNAs to boost functional ncRNA diversity.RNA biology · 2013Review
- Nanometer scale pores similar in size to the entrance of the ribosomal exit cavity are a common feature of large RNAs.RNA (New York, N.Y.) · 2013Article
- A Role for the 2' OH of peptidyl-tRNA substrate in peptide release on the ribosome revealed through RF-mediated rescue.Chemistry & biology · 2012Article
- The chemical versatility of RNA.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2011Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
The ribosome accelerates the rate of peptidyl transfer by >10(6)-fold relative to the background rate. A widely accepted model for this rate enhancement invokes entropic effects whereby the ribosome and the 2'-OH of the peptidyl-tRNA substrate precisely position the reactive moieties through an extensive network of hydrogen bonds that allows proton movement through them. Some studies, however, have called this model into question because they find the 2'-OH of the peptidyl-tRNA to be dispensable for catalysis. Here, we use an in vitro reconstituted translation system to resolve these discrepancies. We find that catalysis is at least 100-fold slower with the dA76-substituted peptidyl-tRNA substrate and that the peptidyl transferase centre undergoes a slow inactivation when the peptidyl-tRNA lacks the 2'-OH group. Additionally, the 2'-OH group was found to be critical for EFTu binding and peptide release. These findings reconcile the conflict in the literature, and support a model where interactions between active site residues and the 2'-OH of A76 of the peptidyl-tRNA are pivotal in orienting substrates in this active site for optimal catalysis.
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Registered trials
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.