Mechanical force releases nascent chain–mediated ribosome arrest in vitro and in vivo
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Summary
A kinetic model is formulated describing how a protein can regulate its own synthesis by the force generated during folding, tuning ribosome activity to structure acquisition by a nascent polypeptide.
- Type
- article
- Published
- 2015-04-23
- Cited by
- 215
- References
- 28
- OpenAlex
- https://openalex.org/W25908824
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:5436434
Keywords
Humanities, Psychology, Sociology, Art
References
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- Theory, analysis, and interpretation of single-molecule force spectroscopy experiments
- Genetically encoded but nonpolypeptide prolyl-tRNA functions in the A site for SecM-mediated ribosomal stall.
- The dynamics of SecM-induced translational stalling
- The geometry of the ribosomal polypeptide exit tunnel.
- Mechanisms of SecM-mediated stalling in the ribosome.
- The ribosomal tunnel as a functional environment for nascent polypeptide folding and translational stalling.
- Single-molecule protein unfolding and translocation by an ATP-fueled proteolytic machine
- Models for the specific adhesion of cells to cells.
- Correlated conformational events in EF-G and the ribosome regulate translocation
- Identification of a SecM segment required for export‐coupled release from elongation arrest
- The Ribosome Modulates Nascent Protein Folding
- ClpX(P) Generates Mechanical Force to Unfold and Translocate Its Protein Substrates
- Hsp70 chaperones accelerate protein translocation and the unfolding of stable protein aggregates by entropic pulling.
- The ribosomal exit tunnel functions as a discriminating gate.
- Widespread regulation of translation by elongation pausing in heat shock
- Nascent peptides that block protein synthesis in bacteria
Cited by
- Probing the structural dynamics of proteins and nucleic acids with optical tweezers
- Dwell-Time Distribution, Long Pausing and Arrest of Single-Ribosome Translation through the mRNA Duplex
- Cotranslational Protein Folding inside the Ribosome Exit Tunnel
- The delicate dance of translation and folding
- Dynamics of peptide chains during co-translational translocation, membrane integration a domain folding
- Nascent chain-monitored remodeling of the Sec machinery for salinity adaptation of marine bacteria
- Insights into Cotranslational Nascent Protein Behavior from Computer Simulations.
- Coupling of mRNA structure rearrangement to ribosome movement during bypassing of non-coding regions
- Physical Origins of Codon Positions That Strongly Influence Cotranslational Folding: A Framework for Controlling Nascent-Protein Folding.
- Integrated in vivo and in vitro nascent chain profiling reveals widespread translational pausing
- Small protein domains fold inside the ribosome exit tunnel
- Trigger Factor Reduces the Force Exerted on the Nascent Chain by a Cotranslationally Folding Protein.
- −1 Programmed Ribosomal Frameshifting as a Force-Dependent Process
- Elongation factor 4 remodels the A-site tRNA on the ribosome
- Mechano-adaptive sensory mechanism of α-catenin under tension
- Parallel computation of genome-scale RNA secondary structure to detect structural constraints on human genome
- A simple DNA handle attachment method for single molecule mechanical manipulation experiments
- Recoding: reprogrammed genetic decoding with an emphasis on antizyme regulatory frameshifting
- Strolling Toward New Concepts.
- Role of mRNA structure in the control of protein folding
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