DOI: 10.1002/pro.5560010308. Purified chaperonin 60 (groEL) interacts with the nonnative states of a multitude of <i>Escherichia coli</i> proteins

Purified chaperonin 60 (groEL) interacts with the nonnative states of a multitude of Escherichia coli proteins

10.1002/pro.5560010308

Crossref journal-article

Wiley

Protein Science (311)

Abstract

AbstractIn vitro experiments employing the soluble proteins from Escherichia coli reveal that about half of them, in their unfolded or partially folded states, but not in their native states, can form stable binary complexes with chaperonin 60 (groEL). These complexes can be isolated by gel filtration chromatography and are efficiently discharged upon the addition of Mg · ATP. Binary complex formation is substantially reduced if chaperonin 60 is presaturated with Rubisco‐I, the folding intermediate of Rubisco, but not with native Rubisco. Binary complex formation is also reduced if the transient species that interact with chaperonin 60 are permitted to progress to more stable states. This implies that the structural elements or motifs that are recognized by chaperonin 60 and that are responsible for binary complex formation are only present or accessible in the unfolded states of proteins or in certain intermediates along their respective folding pathways. Given the high‐affinity binding that we have observed in the present study and the normal cellular abundance of chaperonin 60, we suspect that the folding of most proteins in E. coli does not occur in free solution spontaneously, but instead takes place while they are associated with molecular chaperones.

Bibliography

Viitanen, P. V., Gatenby, A. A., & Lorimer, G. H. (1992). Purified chaperonin 60 (groEL) interacts with the nonnative states of a multitude of Escherichia coli proteins. Protein Science, 1(3), 363â369. Portico.

Authors 3

Paul V. Viitanen (first)
Anthony A. Gatenby (additional)
George H. Lorimer (additional)

References 31 Referenced 202

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Dates

Type	When
Created	15 years, 1 month ago (July 12, 2010, 1:50 a.m.)
Deposited	1 year, 10 months ago (Oct. 23, 2023, 7:17 a.m.)
Indexed	1 month, 3 weeks ago (July 2, 2025, 2:34 p.m.)
Issued	33 years, 5 months ago (March 1, 1992)
Published	33 years, 5 months ago (March 1, 1992)
Published Online	16 years, 7 months ago (Dec. 31, 2008)
Published Print	33 years, 5 months ago (March 1, 1992)

Funders 0

None

BibTeX

@article{Viitanen_1992, title={Purified chaperonin 60 (groEL) interacts with the nonnative states of a multitude of Escherichia coli proteins}, volume={1}, ISSN={1469-896X}, url={http://dx.doi.org/10.1002/pro.5560010308}, DOI={10.1002/pro.5560010308}, number={3}, journal={Protein Science}, publisher={Wiley}, author={Viitanen, Paul V. and Gatenby, Anthony A. and Lorimer, George H.}, year={1992}, month=mar, pages={363–369} }

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