ArticleThe Journal of biological chemistry2014
Chaperones rescue luciferase folding by separating its domains.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 19 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
19 citing papers in PubMed, 37 citations in OpenAlex.
- Quasi-continuous cotranslational compaction and folding of a multidomain protein.Nature communications · 2026Article
- Direct single-molecule visualization of Hsp90-mediated relief of an Hsp70-folding block.Science advances · 2026Article
- Force writes memory: proline isomerization as a molecular memory switch.Biochemical Society transactions · 2025Review
- The human ribosome modulates multidomain protein biogenesis by delaying cotranslational domain docking.Nature structural & molecular biology · 2025Article
- Tandem repeats of highly bioluminescent NanoLuc are refolded noncanonically by the Hsp70 machinery.Protein science : a publication of the Protein Society · 2024Article
- Real-time single-molecule observation of chaperone-assisted protein folding.Science advances · 2022Article
- Mechanical regulation of talin through binding and history-dependent unfolding.Science advances · 2022Article
- Co-Translational Folding of Multi-Domain Proteins.Frontiers in molecular biosciences · 2022Review
- 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
- Mechanical Stability of a Small, Highly-Luminescent Engineered Protein NanoLuc.International journal of molecular sciences · 2020Article
- Piecewise All-Atom SMD Simulations Reveal Key Secondary Structures in Luciferase Unfolding Pathway.Biophysical journal · 2020Article
- Cotranslational folding allows misfolding-prone proteins to circumvent deep kinetic traps.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Energetic dependencies dictate folding mechanism in a complex protein.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Unraveling the Mechanical Unfolding Pathways of a Multidomain Protein: Phosphoglycerate Kinase.Biophysical journal · 2018Article
- Competing Pathways and Multiple Folding Nuclei in a Large Multidomain Protein, Luciferase.Biophysical journal · 2017Article
- Multidomain proteins under force.Nanotechnology · 2017Article
- Single-molecule Force Spectroscopy Reveals the Calcium Dependence of the Alternative Conformations in the Native State of a βγ-Crystallin Protein.The Journal of biological chemistry · 2016Article
- Pharmacological chaperone reshapes the energy landscape for folding and aggregation of the prion protein.Nature communications · 2016Article
- Basement membrane stiffening promotes retinal endothelial activation associated with diabetes.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2016Article
Corrections and comments
- Erratum issued
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Over the last 50 years, significant progress has been made toward understanding how small single-domain proteins fold. However, very little is known about folding mechanisms of medium and large multidomain proteins that predominate the proteomes of all forms of life. Large proteins frequently fold cotranslationally and/or require chaperones. Firefly (Photinus pyralis) luciferase (Luciferase, 550 residues) has been a model of a cotranslationally folding protein whose extremely slow refolding (approximately days) is catalyzed by chaperones. However, the mechanism by which Luciferase misfolds and how chaperones assist Luciferase refolding remains unknown. Here we combine single-molecule force spectroscopy (atomic force microscopy (AFM)/single-molecule force spectroscopy) with steered molecular dynamic computer simulations to unravel the mechanism of chaperone-assisted Luciferase refolding. Our AFM and steered molecular dynamic results show that partially unfolded Luciferase, with the N-terminal domain remaining folded, can refold robustly without chaperones. Complete unfolding causes Luciferase to get trapped in very stable non-native configurations involving interactions between N- and C-terminal residues. However, chaperones allow the completely unfolded Luciferase to refold quickly in AFM experiments, strongly suggesting that chaperones are able to sequester non-natively contacting residues. More generally, we suggest that many chaperones, rather than actively promoting the folding, mimic the ribosomal exit tunnel and physically separate protein domains, allowing them to fold in a cotranslational-like sequential process.
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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.