Cotranslational Protein Folding inside the Ribosome Exit Tunnel
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Summary
It is shown that a small zinc-finger domain protein can fold deep inside the vestibule of the ribosome exit tunnel, which means that the Ribosome itself can provide the kind of sheltered folding environment that chaperones provide for larger proteins.
- Type
- article
- Published
- 2015-08-28
- Cited by
- 245
- References
- 51
- Access
- Open access
- OpenAlex
- https://openalex.org/W1910438362
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:13919253
Keywords
Ribosome, Förster resonance energy transfer, Biophysics, Protein folding, Folding (DSP implementation)
References
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- Thermodynamics of Zn2+ binding to Cys2His2 and Cys2HisCys zinc fingers and a Cys4 transcription factor site.
- Cell-free translation reconstituted with purified components
- Different conformations of nascent polypeptides during translocation across the ER membrane
- Transmembrane Segments Form Tertiary Hairpins in the Folding Vestibule of the Ribosome.
- Sequence-dependent elongation dynamics on macrolide-bound ribosomes
- α-Helical nascent polypeptide chains visualized within distinct regions of the ribosomal exit tunnel
- Irreversible chemical steps control intersubunit dynamics during translation
- Zinc-dependent structure of a single-finger domain of yeast ADR1.
- Structure of the Bacillus subtilis 70S ribosome reveals the basis for species-specific stalling
- Timing is everything: unifying codon translation rates and nascent proteome behavior.
- Cotranslational Folding Inhibits Translocation from Within the Ribosome–Sec61 Translocon Complex
- The dynamics of SecM-induced translational stalling
- Co-translational Folding of an Eukaryotic Multidomain Protein in a Prokaryotic Translation System*
- The geometry of the ribosomal polypeptide exit tunnel.
- Cotranslational protein folding within the ribosome tunnel influences trigger-factor recruitment.
- Preparative scale expression of membrane proteins in Escherichia coli-based continuous exchange cell-free systems
- Tertiary Interactions within the Ribosomal Exit Tunnel
- Replica-exchange molecular dynamics method for protein folding
- Charge-driven dynamics of nascent chain movement through the SecYEG translocon
Cited by
- Kinetic and structural comparison of a protein’s cotranslational folding and refolding pathways
- The dipeptide conformations of all twenty amino acid types in the context of biosynthesis
- Coupling of mRNA structure rearrangement to ribosome movement during bypassing of non-coding regions
- Cotranslational protein folding on the ribosome monitored in real time
- Organization and Regulation of Mitochondrial Protein Synthesis.
- Protein Folding Activity of the Ribosome and Its Implication in Prion Processes
- Caractérisation structurale et fonctionnelle de la peptide déformylase du phage Vp16T
- Translation regulation via nascent polypeptide-mediated ribosome stalling.
- Small protein domains fold inside the ribosome exit tunnel
- Trigger Factor Reduces the Force Exerted on the Nascent Chain by a Cotranslationally Folding Protein.
- A structural ensemble of a ribosome-nascent chain complex during co-translational protein folding
- Co‐ and Post‐Translational Protein Folding in the ER
- Protein Elongation, Co-translational Folding and Targeting.
- How Widespread is Metabolite Sensing by Ribosome-Arresting Nascent Peptides?
- Function of Elongation Factor P in Translation
- The ribosome in action: Tuning of translational efficiency and protein folding
- Recoding: reprogrammed genetic decoding with an emphasis on antizyme regulatory frameshifting
- Dynamic Behavior of Trigger Factor on the Ribosome.
- Strolling Toward New Concepts.
- In vivo aspects of protein folding and quality control
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