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Proceedings of the National Academy of Sciences, Vol 90, 3978-3982, Copyright © 1993 by National Academy of Sciences
K Braig, M Simon, F Furuya, JF Hainfeld and AL Horwich
Chaperonins are oligomeric protein complexes that play an essential role in
the cell, mediating ATP-dependent polypeptide chain folding in a variety of
cellular compartments. They appear to bind early folding intermediates,
preventing their aggregation; in the presence of MgATP and a cochaperonin,
bound polypeptides are released in a stepwise manner, associated with
folding to the native state. Chaperonin complexes appear in the electron
microscope as cylindrical structures, usually composed of two stacked
rings, each containing, by negative staining, an electron dense central
"hole"
ARTICLE
A Polypeptide Bound by the Chaperonin groEL is Localized Within a Central Cavity
6.0 nm in
diameter. We sought to identify the site on the Escherichia coli chaperonin
groEL, where the "molten globule"-like intermediate of dihydrofolate
reductase (DHFR) becomes bound, by examining in the scanning transmission
electron microscope complexes formed between groEL and DHFR molecules
bearing covalently crosslinked 1.4-nm gold clusters. In top views of the
groEL complexes, gold densities were observed in the central region; in
side views, the densities were seen at the end portions of the cylinders,
corresponding to positions within the individual rings. In some cases, two
gold densities were observed in the same groEL complex. We conclude that
folding intermediates are bound inside central cavities within individual
chaperonin rings. In this potentially sequestered location, folding
intermediates with a compact conformation can be bound at multiple sites by
surrounding monomeric members of the ring; localization of folding within
the cavity could also facilitate rebinding of structures that initially
fail to incorporate properly into the folding protein.
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