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Comment
. 2015 Dec 15;112(50):E6833-4.
doi: 10.1073/pnas.1520474112. Epub 2015 Nov 24.

Reply to Marchenko et al.: Flux analysis of GroEL-assisted protein folding/unfolding

David S Libich  1 , Vitali Tugarinov  1 , G Marius Clore  2
Affiliations
Comment

Reply to Marchenko et al.: Flux analysis of GroEL-assisted protein folding/unfolding

David S Libich et al. Proc Natl Acad Sci U S A. .
No abstract available

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Fig. 1.
Fig. 1.
Fluxes at equilibrium for the F to I interconversion through the GroEL-assisted and unassisted pathways. (A) Total (green), GroEL-assisted (blue), and GroEL-unassisted (red) fluxes as a function of total GroEL concentration. FluxtotalF↔I is given by the sum of the fluxes through the GroEL-assisted and unassisted pathways. Note that the decrease in the GroEL-unassisted flux with increasing GroEL concentration is due to the concomitant decrease in the concentration of the free folded state F. (B) Ratio of GroEL-assisted to unassisted fluxes. Inset in B depicts the reaction scheme and rate constants (1) for the direct, unassisted (red) and GroEL-assisted (blue) interconversion between the F and I states of the metastable SH3 domain. Concentrations of all species at equilibrium were calculated by integrating the differential equations describing the reaction scheme shown in Inset until the steady state is reached (6). The total concentration of SH3 domain is 100 μM. The total concentration of GroEL is expressed in terms of the GroEL 14mer.
See this image and copyright information in PMC

Comment on

References

    1. Libich DS, Tugarinov V, Clore GM. Intrinsic unfoldase/foldase activity of the chaperonin GroEL directly demonstrated using multinuclear relaxation-based NMR. Proc Natl Acad Sci USA. 2015;112(29):8817–8823. - PMC - PubMed
    1. Marchenko NY, Marchenkov VV, Semisotnov GV, Finkelstein AV. Strict experimental evidence that apo-chaperonin GroEL does not accelerate protein folding, although it does accelerate one of its steps. Proc Natl Acad Sci USA. 2015;112:E6831–E6832. - PMC - PubMed
    1. Marchenkov VV, et al. [The interaction of the GroEL chaperone with early kinetic intermediates of renaturing proteins inhibits the formation of their native structure] Biofizika. 2004;49(6):987–994. Russian. - PubMed
    1. Hammes GG, Chang Y-C, Oas TG. Conformational selection or induced fit: a flux description of reaction mechanism. Proc Natl Acad Sci USA. 2009;106(33):13737–13741. - PMC - PubMed
    1. Chatellier J, Hill F, Lund PA, Fersht AR. In vivo activities of GroEL minichaperones. Proc Natl Acad Sci USA. 1998;95(17):9861–9866. - PMC - PubMed

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