Transient association of newly synthesized unfolded proteins with the heat-shock GroEL protein
- 1 November 1988
- journal article
- Published by Springer Nature in Nature
- Vol. 336 (6196) , 254-257
- https://doi.org/10.1038/336254a0
Abstract
It has been suggested that newly synthesized proteins are maintained in their unfolded state by cellular ATP-driven factors which may prevent or reverse the formation of misfolded structures or promote the correct assembly of oligomeric proteins or post-translational secretion. Using a photocross-linking approach, we have identified the 20S heat-shock GroEL protein as the major cytosolic component which forms a complex with the unfolded newly synthesized pre-beta-lactamase or chloramphenicol acetyltransferase in Escherichia coli. Dissociation of these complexes is ATP-dependent. The unfolded state of pre-beta-lactamase, maintained by the transient interaction with GroEL, may be essential for the secretion of this protein.Keywords
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