ArticleProtein science : a publication of the Protein Society2000
Assisted folding of D-glyceraldehyde-3-phosphate dehydrogenase by trigger factor.
Article in Protein science : a publication of the Protein Society, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- Chaperone dependency during biogenesis does not correlate with chaperone dependency during refolding.Molecular systems biology · 2026Article
- Chaperone Dependency during Primary Protein Biogenesis Does Not Correlate with Chaperone Dependency duringbioRxiv : the preprint server for biology · 2025Article
- A truncated variant of the ribosome-associated trigger factor specifically contributes to plant chloroplast ribosome biogenesis.Nature communications · 2025Article
- Article
- Pulling Forces Differentially Affect Refolding Pathways Due to Entangled Misfolded States in SARS-CoV-1 and SARS-CoV-2 Receptor Binding Domain.Biomolecules · 2024Article
- Article
- Protein folding in vitro and in the cell: From a solitary journey to a team effort.Biophysical chemistry · 2022Review
- Trigger factor both holds and folds its client proteins.Nature communications · 2022Article
- Article
- Nonrefoldability is Pervasive Across theJournal of the American Chemical Society · 2021Article
- Mechanisms of Cotranslational Protein Maturation in Bacteria.Frontiers in molecular biosciences · 2021Review
- Chaperone action of a cofactor in protein folding.Protein science : a publication of the Protein Society · 2020Article
- The Role of Plastidic Trigger Factor Serving Protein Biogenesis in Green Algae and Land Plants.Plant physiology · 2019Article
- Forces Driving Chaperone Action.Cell · 2016Article
- Molecular chaperones are nanomachines that catalytically unfold misfolded and alternatively folded proteins.Cellular and molecular life sciences : CMLS · 2014Review
- Hydrophobic collapse of trigger factor monomer in solution.PloS one · 2013Article
- Beta-barrel scaffold of fluorescent proteins: folding, stability and role in chromophore formation.International review of cell and molecular biology · 2013Review
- cpSRP43 is a novel chaperone specific for light-harvesting chlorophyll a,b-binding proteins.The Journal of biological chemistry · 2010Article
- Article
- CP12 from Chlamydomonas reinhardtii, a permanent specific "chaperone-like" protein of glyceraldehyde-3-phosphate dehydrogenase.The Journal of biological chemistry · 2009Article
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Authors and funding
4 authors.
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No grant is acknowledged in the PubMed record.
Abstract
The Escherichia coli trigger factor is a peptidyl-prolyl cis-trans isomerase that catalyzes proline-limited protein folding extremely well. Here, refolding of D-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) in the presence of trigger factor was investigated. The regain of activity of GAPDH was markedly increased by trigger factor after either long- or short-term denaturation, and detectable aggregation of GAPDH intermediates was prevented. In both cases, time courses of refolding of GAPDH were decelerated by trigger factor. The reactivation yield of GAPDH showed a slow down-turn when molar ratios of trigger factor to GAPDH were above 5, due to tight binding between trigger factor and GAPDH intermediates. Such inactive bound GAPDH could be partially rescued from trigger factor by addition of reduced alphaLA as competitor, by further diluting the refolding mixture, or by disrupting hydrophobic interactions in the complexes. A model for trigger factor assisted refolding of GAPDH is proposed. We also suggest that assisted refolding of GAPDH is due mainly to the chaperone function of trigger factor.
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