ArticleJournal of the American Chemical Society2018
Origins of the Mechanochemical Coupling of Peptide Bond Formation to Protein Synthesis.
Article in Journal of the American Chemical Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- Protein entanglement misfolding influences whether proteins undergo proteasomal degradation or persist in near-native misfolded states.Nature communications · 2026Article
- Mechanical forces regulate the composition and fate of stalled nascent chains.Molecular cell · 2026Article
- Co-translational ribosome pairing enables native assembly of misfolding-prone subunits.Nature communications · 2025Article
- Structures of Polyhydroxyalkanoate Synthase PhaC from Aeromonas caviae, Producing Biodegradable Plastics.Angewandte Chemie (International ed. in English) · 2025Article
- Protein misfolding involving entanglements providesa structural explanation for the origin of stretched-exponential refolding kinetics.Science advances · 2025Article
- Synthesis of Metal-Organic Cages via Orthogonal Bond Cleavage in 3D Metal-Organic Frameworks.Journal of the American Chemical Society · 2024Article
- How synonymous mutations alter enzyme structure and function over long timescales.Nature chemistry · 2023Article
- Coordination of -1 programmed ribosomal frameshifting by transcript and nascent chain features revealed by deep mutational scanning.Nucleic acids research · 2021Article
- Peptidyl transferase center decompaction and structural constraints during early protein elongation on the ribosome.Scientific reports · 2021Article
- Ribosome Elongation Kinetics of Consecutively Charged Residues Are Coupled to Electrostatic Force.Biochemistry · 2021Article
- Mechanical Forces Have a Range of Effects on the Rate of Ribosome Catalyzed Peptidyl Transfer Depending on Direction.The journal of physical chemistry. B · 2021Article
- Co-translational folding of nascent polypeptides: Multi-layered mechanisms for the efficient biogenesis of functional proteins.BioEssays : news and reviews in molecular, cellular and developmental biology · 2021Article
- Force transduction creates long-ranged coupling in ribosomes stalled by arrest peptides.Biophysical journal · 2021Article
- The many flavours of mechanochemistry and its plausible conceptual underpinnings.Nature reviews. Chemistry · 2021Review
- Gradual compaction of the nascent peptide during cotranslational folding on the ribosome.eLife · 2020Article
- Novel Methodologies for Chemical Activation in Organic Synthesis under Solvent-Free Reaction Conditions.Molecules (Basel, Switzerland) · 2020Review
- Cotranslational folding cooperativity of contiguous domains of α-spectrin.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Forcing the ribosome to change its message.The Journal of biological chemistry · 2020Article
- Electrostatic Interactions Govern Extreme Nascent Protein Ejection Times from Ribosomes and Can Delay Ribosome Recycling.Journal of the American Chemical Society · 2020Article
- Review
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7 authors.
Funding
Abstract
Mechanical forces acting on the ribosome can alter the speed of protein synthesis, indicating that mechanochemistry can contribute to translation control of gene expression. The naturally occurring sources of these mechanical forces, the mechanism by which they are transmitted 10 nm to the ribosome's catalytic core, and how they influence peptide bond formation rates are largely unknown. Here, we identify a new source of mechanical force acting on the ribosome by using in situ experimental measurements of changes in nascent-chain extension in the exit tunnel in conjunction with all-atom and coarse-grained computer simulations. We demonstrate that when the number of residues composing a nascent chain increases, its unstructured segments outside the ribosome exit tunnel generate piconewtons of force that are fully transmitted to the ribosome's P-site. The route of force transmission is shown to be through the nascent polypetide's backbone, not through the wall of the ribosome's exit tunnel. Utilizing quantum mechanical calculations we find that a consequence of such a pulling force is to decrease the transition state free energy barrier to peptide bond formation, indicating that the elongation of a nascent chain can accelerate translation. Since nascent protein segments can start out as largely unfolded structural ensembles, these results suggest a pulling force is present during protein synthesis that can modulate translation speed. The mechanism of force transmission we have identified and its consequences for peptide bond formation should be relevant regardless of the source of the pulling force.
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