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PMID:2192863

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Citation

Laminet, AA, Ziegelhoffer, T, Georgopoulos, C and Plückthun, A (1990) The Escherichia coli heat shock proteins GroEL and GroES modulate the folding of the beta-lactamase precursor. EMBO J. 9:2315-9

Abstract

One of the fundamental problems in biochemistry is the role of accessory proteins in the process of protein folding. The Escherichia coli heat shock protein complex GroEL/ES has been suggested to be a 'chaperonin' and be involved in both oligomer assembly as well as protein transport through the membrane. We show here that the folding of the purified precursor of beta-lactamase is inhibited by purified GroEL or the GroEL/ES complex with a stoichiometry of one particle per molecule of pre-beta-lactamase. Purified GroES alone has no effect on folding. After Mg2+ ATP addition folding resumes and the yield of active enzyme is higher than in the absence of GroEL or GroEL/ES. Unexpectedly, GroEL or GroEL/ES, when added to folded pre-beta-lactamase, lead to an apparent net 'unfolding', probably to a collapsed state of the protein, which can be reversed by the addition of Mg2+ ATP. The reversible and Mg2+ ATP-dependent association of GroEL/ES with non-native proteins might explain its postulated role in both protein transport and oligomer assembly.

Links

PubMed PMC551958

Keywords

Enzyme Precursors/metabolism; Escherichia coli/metabolism; Heat-Shock Proteins/metabolism; Kinetics; Peptide Mapping; Protein Conformation; Trypsin; beta-Lactamases/metabolism

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

ECOLI:CH10

GO:0006457: protein folding

ECO:0000314:

P

Figure 2a shows the effect of addition of GroES and ATP to a arrested GroEL protein folding of pre-beta-lactamase. Enzyme function dramatically increases after addition,suggesting GroES is required for proper protein folding

complete
CACAO 8869

ECOLI:CH10

involved_in

GO:0006457: protein folding

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

See also

References

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