Molecular chaperone machines: Chaperone activities of the cyclophilin Cyp-40 and the steroid aporeceptor-associated protein p23

Science

Volumn 274, Issue 5293, 1996, Pages 1718-1720

  Freeman, Brian C ^a   Toft, David O ^b   Morimoto, Richard I ^a  

^a NORTHWESTERN UNIVERSITY   (United States)

^b MAYO GRADUATE SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYCLOPHILIN; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; PROTEIN P23; STEROID RECEPTOR; UNCLASSIFIED DRUG;

ARTICLE; MOLECULAR DYNAMICS; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN PURIFICATION; RECEPTOR AFFINITY;

AMINO ACID ISOMERASES; BETA-GALACTOSIDASE; CARRIER PROTEINS; CYCLOPHILINS; HEAT; HEAT-SHOCK PROTEINS; HSC70 HEAT-SHOCK PROTEINS; HSP40 HEAT-SHOCK PROTEINS; HSP70 HEAT-SHOCK PROTEINS; MOLECULAR CHAPERONES; PEPTIDYLPROLYL ISOMERASE; PHOSPHOPROTEINS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; SOLUBILITY;

EUKARYOTA;

EID: 0029852712     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.274.5293.1718     Document Type: Article

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29. 2, 10 mM dithiothreitol, and 1 mM adenosine triphosphate] to a final concentration of 3.4 nM β-Gal, and supplemented with BSA, Hsp90, Hsp70, p60, Cyp-40, Hdj-1, or p23, or various combinations of chaperones. The refolding reactions were incubated at 37°C for 240 min and aliquots (11 μl) were taken at various time points. The percent enzyme activity was determined after incubation with orthonitrophenyl galactoside and measurement of absorbance at 412 nm. The results are presented as percent enzyme activity relative to the same amount of native β-Gal (3.4 nM) in refolding buffer containing BSA (1.6 μM), The molecular chaperones Hsp90, Hsp70, and Hdj-1 were purified to homogeneity as described (6). Cyp-40 [L. J. Kieffer et al., J. Biol. Chem. 268, 12303 (1993)] was purified with a Resource Q column and used as a glutathione-S-transferase (GST) fusion protein.
30. The p60 [D. F. Smith et al., Mol. Cell. Biol. 13, 869 (1993) ] and p23 [J. L. Johnson, T. G. Bieto, C. J. Krco, D. O. Toft, ibid. 14, 1956 (1994)] proteins were recombinantly expressed and purified by sequential passages over DEAE, Resource Q, and Superdex-200 columns (Pharmacia Biotech).
31. The p60 [D. F. Smith et al., Mol. Cell. Biol. 13, 869 (1993) ] and p23 [J. L. Johnson, T. G. Bieto, C. J. Krco, D. O. Toft, ibid. 14, 1956 (1994)] proteins were recombinantly expressed and purified by sequential passages over DEAE, Resource Q, and Superdex-200 columns (Pharmacia Biotech).
32. B. C. Freeman and R. I. Morimoto, unpublished observations
33. The folded state of denatured β-Gal diluted into BSA, Hsc70, p60, Cyp-40, Hdj-1, or p23 was characterized by electrophoresis on native 4% polyacrylamide Na-borate (0.1 M sodium acetate and 0.1 M boric acid) gels at 4°C at 1 mm/min (6) or by separation of the soluble and insoluble fractions of β-Gal by centrifugation at 13,000 rpm for 5 min and separation with 10% SDS-PAGE. The β-Gal was detected by protein immunoblot analysis after electroblotting onto nitrocellulose, incubation with an antibody to β-Gal (anti-β-Gal), and detection by ECL (Amersham).
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36. Supported by NIH grant GM38109. B.C.F. was supported by a National Research Service Award predoctoral training grant. We thank R. Holmgren for anti-β-Gal and D. Montgomery and S. Mathur for comments.