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PMID: 2192863 Published · ppublish English Journal Article

The Escherichia coli heat shock proteins GroEL and GroES modulate the folding of the beta-lactamase precursor.

The EMBO journal ·Vol. 9 ·No. 7 ·1990-07-00 ·Pages 2315-9

Laminet AA, Ziegelhoffer T, Georgopoulos C, Plückthun A

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.

MeSH Terms
Enzyme Precursors/metabolism Escherichia coli/metabolism Heat-Shock Proteins/metabolism Kinetics Peptide Mapping Protein Conformation Trypsin beta-Lactamases/metabolism
Chemicals
Enzyme Precursors Heat-Shock Proteins Trypsin pre-beta-lactamase beta-Lactamases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Laminet A A
Genzentrum der Universität München, Max-Planck-Institut für Biochemie, Martinsried, FRG.
Ziegelhoffer T
Georgopoulos C
Plückthun A
References (44)
44 references, click to expand
  1. Transient association of newly synthesized unfolded proteins with the heat-shock GroEL protein.
    Nature. 1988 Nov 17;336(6196):254-7 PMID: 2904124
  2. Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis.
    Nature. 1989 Sep 14;341(6238):125-30 PMID: 2528694
  3. The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures.
    J Bacteriol. 1989 Mar;171(3):1379-85 PMID: 2563997
  4. Molecular chaperones: proteins essential for the biogenesis of some macromolecular structures.
    Trends Biochem Sci. 1989 Aug;14(8):339-42 PMID: 2572080
  5. Polypeptide chain binding proteins: catalysts of protein folding and related processes in cells.
    Cell. 1989 Nov 17;59(4):591-601 PMID: 2573430
  6. Effects of mutations in heat-shock genes groES and groEL on protein export in Escherichia coli.
    EMBO J. 1989 Nov;8(11):3517-21 PMID: 2573517
  7. Three pure chaperone proteins of Escherichia coli--SecB, trigger factor and GroEL--form soluble complexes with precursor proteins in vitro.
    EMBO J. 1989 Sep;8(9):2703-9 PMID: 2531087
  8. The molecular chaperone concept.
    Biochem Soc Symp. 1989;55:145-53 PMID: 2695089
  9. The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure.
    Proteins. 1989;6(2):87-103 PMID: 2695928
  10. The Escherichia coli groE chaperonins.
    Semin Cell Biol. 1990 Feb;1(1):19-25 PMID: 1983267
  11. Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP.
    Nature. 1989 Dec 21-28;342(6252):884-9 PMID: 10532860
  12. Principles that govern the folding of protein chains.
    Science. 1973 Jul 20;181(4096):223-30 PMID: 4124164
  13. Novel method for detection of beta-lactamases by using a chromogenic cephalosporin substrate.
    Antimicrob Agents Chemother. 1972 Apr;1(4):283-8 PMID: 4208895
  14. Experimental studies of protein folding and unfolding.
    Prog Biophys Mol Biol. 1978;33(3):231-97 PMID: 358273
  15. Isolation and characterization of the host protein groE involved in bacteriophage lambda assembly.
    J Mol Biol. 1979 Apr 15;129(3):359-73 PMID: 379349
  16. Purification and properties of groE, a host protein involved in bacteriophage assembly.
    J Mol Biol. 1979 Apr 15;129(3):375-92 PMID: 379350
  17. A rapid, sensitive method for detection of alkaline phosphatase-conjugated anti-antibody on Western blots.
    Anal Biochem. 1984 Jan;136(1):175-9 PMID: 6424501
  18. Protein translocation across the endoplasmic reticulum.
    Cell. 1984 Aug;38(1):5-8 PMID: 6088076
  19. The signal sequence of nascent preprolactin interacts with the 54K polypeptide of the signal recognition particle.
    Nature. 1986 Apr 17-23;320(6063):634-6 PMID: 3010127
  20. Peptide and protein molecular weight determination by electrophoresis using a high-molarity tris buffer system without urea.
    Anal Biochem. 1986 May 15;155(1):83-8 PMID: 3454661
  21. Binding of a specific ligand inhibits import of a purified precursor protein into mitochondria.
    Nature. 1986 Jul 17-23;322(6076):228-32 PMID: 3016548
  22. Purification and properties of the groES morphogenetic protein of Escherichia coli.
    J Biol Chem. 1986 Sep 15;261(26):12414-9 PMID: 3017973
  23. Correlation of competence for export with lack of tertiary structure of the mature species: a study in vivo of maltose-binding protein in E. coli.
    Cell. 1986 Sep 12;46(6):921-8 PMID: 3530497
  24. Speculations on the functions of the major heat shock and glucose-regulated proteins.
    Cell. 1986 Sep 26;46(7):959-61 PMID: 2944601
  25. Suppression of a signal sequence mutation by an amino acid substitution in the mature portion of the maltose-binding protein.
    J Bacteriol. 1987 May;169(5):1794-800 PMID: 3553148
  26. Trigger factor: a soluble protein that folds pro-OmpA into a membrane-assembly-competent form.
    Proc Natl Acad Sci U S A. 1987 Aug;84(15):5216-20 PMID: 3299381
  27. Proteins as molecular chaperones.
    Nature. 1987 Jul 30-Aug 5;328(6129):378-9 PMID: 3112578
  28. Catalysis of protein folding by prolyl isomerase.
    Nature. 1987 Sep 17-23;329(6136):268-70 PMID: 3306408
  29. A highly evolutionarily conserved mitochondrial protein is structurally related to the protein encoded by the Escherichia coli groEL gene.
    Mol Cell Biol. 1988 Jan;8(1):371-80 PMID: 2892128
  30. Folding and association of proteins.
    Prog Biophys Mol Biol. 1987;49(2-3):117-237 PMID: 3327098
  31. A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides.
    Nature. 1988 Apr 28;332(6167):800-5 PMID: 3282178
  32. 70K heat shock related proteins stimulate protein translocation into microsomes.
    Nature. 1988 Apr 28;332(6167):805-10 PMID: 3282179
  33. The antifolding activity of SecB promotes the export of the E. coli maltose-binding protein.
    Cell. 1988 Apr 22;53(2):273-83 PMID: 2834066
  34. Homologous plant and bacterial proteins chaperone oligomeric protein assembly.
    Nature. 1988 May 26;333(6171):330-4 PMID: 2897629
  35. Effects of Escherichia coli secB mutations on pre-maltose binding protein conformation and export kinetics.
    J Biol Chem. 1988 Aug 15;263(23):11554-8 PMID: 3042772
  36. ProOmpA spontaneously folds in a membrane assembly competent state which trigger factor stabilizes.
    EMBO J. 1988 Jun;7(6):1831-5 PMID: 3049077
  37. The 'molten globule' state is involved in the translocation of proteins across membranes?
    FEBS Lett. 1988 Oct 10;238(2):231-4 PMID: 3049159
  38. Defective co-translational formation of disulphide bonds in protein disulphide-isomerase-deficient microsomes.
    Nature. 1988 Oct 13;335(6191):649-51 PMID: 3173483
  39. Seventy-kilodalton heat shock proteins and an additional component from reticulocyte lysate stimulate import of M13 procoat protein into microsomes.
    EMBO J. 1988 Sep;7(9):2875-80 PMID: 3181144
  40. Homology of 54K protein of signal-recognition particle, docking protein and two E. coli proteins with putative GTP-binding domains.
    Nature. 1989 Aug 10;340(6233):478-82 PMID: 2502717
  41. Model for signal sequence recognition from amino-acid sequence of 54K subunit of signal recognition particle.
    Nature. 1989 Aug 10;340(6233):482-6 PMID: 2502718
  42. Peptide binding and release by proteins implicated as catalysts of protein assembly.
    Science. 1989 Jul 28;245(4916):385-90 PMID: 2756425
  43. The precursor of beta-lactamase: purification, properties and folding kinetics.
    EMBO J. 1989 May;8(5):1469-77 PMID: 2670555
  44. GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli.
    Nature. 1989 Jan 5;337(6202):44-7 PMID: 2562907
Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1990-07-00
Pages
2315-9
Language
English
Region
England
NLM ID
8208664
PMCID
PMC551958
Subset
IM
External Links
PubMed source PMC Full Text View journal details
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