ArticleProtein science : a publication of the Protein Society1996
Significant hydrogen exchange protection in GroEL-bound DHFR is maintained during iterative rounds of substrate cycling.
Article in Protein science : a publication of the Protein Society, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 63 citations in OpenAlex.
- Folding trajectories of human dihydrofolate reductase inside the GroEL GroES chaperonin cavity and free in solution.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Scope and utility of hydrogen exchange as a tool for mapping landscapes.Protein science : a publication of the Protein Society · 2007Article
- Disulfide formation as a probe of folding in GroEL-GroES reveals correct formation of long-range bonds and editing of incorrect short-range ones.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Electron paramagnetic resonance and fluorescence studies of the conformation of aspartate aminotransferase bound to GroEL.The protein journal · 2005Article
- Direct NMR observation of a substrate protein bound to the chaperonin GroEL.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- Expansion and compression of a protein folding intermediate by GroEL.Molecular cell · 2004Article
- The unfolding action of GroEL on a protein substrate.Biophysical journal · 2004Article
- Thermostability of endo-1,4-beta-xylanase II from Trichoderma reesei studied by electrospray ionization Fourier-transform ion cyclotron resonance MS, hydrogen/deuterium-exchange reactions and dynamic light scattering.The Biochemical journal · 2001Article
- Chaperone rings in protein folding and degradation.Proceedings of the National Academy of Sciences of the United States of America · 1999Review
- Chaperonin function: folding by forced unfolding.Science (New York, N.Y.) · 1999Article
- The chaperonin cycle cannot substitute for prolyl isomerase activity, but GroEL alone promotes productive folding of a cyclophilin-sensitive substrate to a cyclophilin-resistant form.The EMBO journal · 1997Article
- Hydrogen exchange properties of proteins in native and denatured states monitored by mass spectrometry and NMR.Protein science : a publication of the Protein Society · 1997Article
- Protein folding: how the mechanism of GroEL action is defined by kinetics.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
- GroEL-mediated protein folding: making the impossible, possible.Critical reviews in biochemistry and molecular biologyReview
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5 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
An unresolved key issue in the mechanism of protein folding assisted by the molecular chaperone GroEL is the nature of the substrate protein bound to the chaperonin at different stages of its reaction cycle. Here we describe the conformational properties of human dihydrofolate reductase (DHFR) bound to GroEL at different stages of its ATP-driven folding reaction, determined by hydrogen exchange labeling and electrospray ionization mass spectrometry. Considerable protection involving about 20 hydrogens is observed in DHFR bound to GroEL in the absence of ATP. Analysis of the line width of peaks in the mass spectra, together with fluorescence quenching and ANS binding studies, suggest that the bound DHFR is partially folded, but contains stable structure in a small region of the polypeptide chain. DHFR rebound to GroEL 3 min after initiating its folding by the addition of MgATP was also examined by hydrogen exchange, fluorescence quenching, and ANS binding. The results indicate that the extent of protection of the substrate protein rebound to GroEL is indistinguishable from that of the initial bound state. Despite this, small differences in the quenching coefficient and ANS binding properties are observed in the rebound state. On the basis of these results, we suggest that GroEL-assisted folding of DHFR occurs by minor structural adjustments to the partially folded substrate protein during iterative cycling, rather than by complete unfolding of this protein substrate on the chaperonin surface.
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