Abstract
The conformation of a three-disulphide derivative of bovine α-lactalbumin bound to the molecular chaperone GroEL has been investigated by monitoring directly its hydrogen exchange kinetics using electrospray ionization mass spectrometry. The bound protein is weakly protected from exchange to an extent closely similar to that of an uncomplexed molten globule state of the three-disulphide protein. Binding to GroEL in this system appears to involve relatively disordered partly folded states resembling intermediates formed in the very early stages of kinetic folding of many proteins in vitro.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Jaenicke, R. Curr. Opin. struct. Biol. 3, 104–112 (1993).
Hartl, F. U., Hlodan, R. & Langer, T. Trends biochem. Sci. 19, 20–25 (1994).
Langer, T. et al. Nature 356, 683–689 (1992).
Englander, S. W. & Mayne, L. A. Rev. biophys. biomolec. Struct. 21, 243–265 (1992).
Woodward, C. K. Curr. Opin. struct. Biol. 4, 112–116 (1994).
Smith, R. D., Loo, J. A., Edmonds, C. G., Barinaga, C. J. & Udseth, H. R. Analyt. Chem. 62, 882–889 (1990).
Zahn, R., Spitzfaden, C., Ottiger, M., Wüthrich, K. & Plückthun, A. Nature 368, 261–265 (1994).
Miranker, A., Robinson, C. V., Radford, S. E., Aplin, R. T. & Dobson, C. M. Science 262, 896–899 (1993).
Landry, S. J. & Gierasch, L. M. Biochemistry 30, 7359–7362 (1991).
Langer, T., Pfeifer, G., Martin, J., Baumeister, W. & Hartl, F. U. EMBO J. 11, 4757–4765 (1992).
Braig, K., Simon, M., Furuya, F., Hainfeld, J. F. & Horwich, A. L. Proc. natn. Acad. Sci. U.S.A. 90, 3978–3982 (1993).
Ishii, N., Taguchi, H., Sasabe, H. & Yoshida, M. J. molec. Biol. 236, 691–696 (1994).
Chen, S. et al. Nature 371, 261–264 (1994).
Schmidt, M. & Buchner, J. J. biol. Chem. 267, 16829–16833 (1992).
Richarme, G. & Kohiyama, M. J. biol. Chem. 269, 7095–7098 (1994).
Martin, J. et al. Nature 352, 36–42 (1991).
Flynn, G. C., Beckers, C. J. M., Baase, W. A. & Dahlquist, F. W. Proc. natn. Acad. Sci. U.S.A. 90, 10826–10830 (1993).
Hayer-Hartl, M. K., Ewbank, J. J., Creighton, T. E. & Hartl, F. U. EMBO J. 13, 3192–3202 (1994).
Okazaki, A., Ikura, T., Nikaido, K. & Kuwajima, K. Nature struct. Biol. 1, 439–446 (1994).
Bychkova, V. E. & Ptitsyn, O. B. Chemtracts Biochem. molec. Biol. 4, 133–163 (1993).
Kuwajima, K. Proteins Struct. Funct. Genet. 6, 87–103 (1989).
Ewbank, J. J. & Creighton, T. E. Nature 350, 518–520 (1989).
Acharya, K. R., Stuart, D. I., Walker, N. P. C., Lewis, M. & Phillips, D. C. J. molec. Biol. 208, 99–127 (1989).
Acharya, K. R., Ren, J., Stuart, D. I., Phillips, D. C. & Fenna, R. E. J. molec. Biol. 221, 571–581 (1991).
Alexandrescu, A. T., Evans, P. A., Pitkeathly, M., Baum, J. & Dobson, C. M. Biochemistry 32, 1707–1718 (1993).
Jeng, M.-F. & Englander, S. W. J. molec. Biol. 221, 1045–1061 (1991).
Chyan, C. L., Wormald, C., Dobson, C. M., Evans, P. A. & Baum, J. Biochemistry 32, 5681–5691 (1993).
Dobson, C. M., Evans, P. A. & Radford, S. E. Trends biochem. Sci. 19, 31–37 (1994).
Radford, S. E., Dobson, C. M. & Evans, P. A. Nature 358, 302–307 (1992).
Loo, J. A., Ogorzalek Loo, R. R., Udseth, H. R., Edmonds, C. G. & Smith, R. D. Rap. Commun. Mass Spectrom. 5, 101–105 (1991).
Light-Wahl, K. J., Winger, B. E. & Smith, R. D. J. Am. chem. Soc. 115, 5869–5870 (1993).
Shewale, J. G., Sinha, S. K. & Brew, K. J. biol. Chem. 259, 4947–4956 (1984).
Wang, M. et al. J. biol. Chem. 264, 21116–21121 (1989).
Kronman, M. J. CRC Crit. Rev. Biochem. molec. Biol. 24, 565–667 (1989).
Chowdhury, S. K., Katta, V. & Chait, B. T. J. Am. chem. Soc. 112, 9012–9013 (1990).
Radford, S. E., Woolfson, D. N., Martin, S. R., Lowe, G. & Dobson, C. M. Biochem. J. 273, 211–217 (1991).
Pederson, T. G., Thomsen, N. K., Andersen, K. V., Madsen, J. C. & Poulsen, F. M. J. molec. Biol. 230, 651–666 (1993).
Radford, S. E., Buck, M., Topping, K. D., Dobson, C. M. & Evans, P. A. Proteins Struct. Funct. Genet. 14, 237–248 (1992).
Bai, Y., Milne, J. S., Mayne, L. & Englander, S. W. Proteins Struct. Funct. Genet. 17, 75–86 (1993).
Connelly, G. P., Bai, Y., Jeng, M.-F. & Englander, S. W. Proteins Struct. Funct. Genet. 17, 87–92 (1993).
Buck, M., Radford, S. E. & Dobson, C. M. J. molec. Biol. 237, 247–254 (1994).
Hughson, F. M., Wright, P. E. & Baldwin, R. L. Science 249, 1544–1548 (1990).
Horovitz, A., Bochkareva, E. S., Kovalenko, O. & Girshovich, A. S. J. molec. biol. 231, 58–64 (1993).
Azem, A., Diamant, S. & Goloubinoff, P. Biochemistry 33, 6671–6675 (1994).
Lissin, N. M. & Hemmingsen, S. M. FEBS Lett. 324, 41–44 (1993).
Ewbank, J. J. & Creighton, T. E. Biochemistry 32, 3694–3707 (1993).
Creighton, T. E. & Ewbank, J. J. (1994).49. Ikeguchi, M. & Sugai, S. Biochemistry 31, 12695–12700 (1992).
Bychkova, V. E., Pain, R. H. & Ptitsyn, O. B. FEBS Lett. 238, 231–234 (1988).
Ikeguchi, M., Sugai, S., Fujino, M., Sugawara, T. & Kuwajima, K. Biochemistry 31, 12695–12700 (1992).
Eyles, S. J., Radford, S. E., Robinson, C. V. & Dobson, C. M. Biochemistry 33, 1534–1538 (1994).
Aramini, J. M. et al. Biochemistry 31, 6761–6768 (1992).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Robinson, C., Groß, M., Eyles, S. et al. Conformation of GroEL-bound α-lactalbumin probed by mass spectrometry. Nature 372, 646–651 (1994). https://doi.org/10.1038/372646a0
Issue Date:
DOI: https://doi.org/10.1038/372646a0
This article is cited by
-
Quantitative Evaluation of Native Protein Folds and Assemblies by Hydrogen Deuterium Exchange Mass Spectrometry (HDX-MS)
Journal of the American Society for Mass Spectrometry (2019)
-
Defining Gas-Phase Fragmentation Propensities of Intact Proteins During Native Top-Down Mass Spectrometry
Journal of the American Society for Mass Spectrometry (2017)
-
Watching and weighting—chaperone complexes in action
Nature Methods (2005)
-
Monitoring macromolecular complexes involved in the chaperonin-assisted protein folding cycle by mass spectrometry
Nature Methods (2005)
-
The oligomeric structure of GroEL/GroES is required for biologically significant chaperonin function in protein folding
Nature Structural Biology (1998)
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.