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 secretion1–6. 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-β-lactamase or chloramphenicol acetyltransferase in Escherichia coli. Dissociation of these com-plexes is ATP-dependent. The unfolded state of pre-β-lactamase, maintained by the transient interaction with GroEL, may be essen-tial for the secretion of this protein.
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Bochkareva, E., Lissin, N. & Girshovich, A. Transient association of newly synthesized unfolded proteins with the heat-shock GroEL protein. Nature 336, 254–257 (1988). https://doi.org/10.1038/336254a0
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DOI: https://doi.org/10.1038/336254a0
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