메뉴 건너뛰기




Volumn 49, Issue 6, 2010, Pages 1137-1145

Chaperone activity of Cyp18 through hydrophobic condensation that enables rescue of transient misfolded molten globule intermediates

Author keywords

[No Author keywords available]

Indexed keywords

BINDING DATA; CHAPERONE ACTIVITY; CITRATE SYNTHASE; CYCLOPHILIN; FOLDING REACTIONS; HUMAN CARBONIC ANHYDRASE II; ISOMERASES; MISFOLDING; MOLTEN GLOBULE; MULTI DOMAINS; NATIVE PROTEINS; NATIVE-STATE PROTEIN; PROTEIN SUBSTRATE; REFOLDING; SINGLE DOMAINS; SUBSTRATE PROTEINS;

EID: 76749168158     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi901997q     Document Type: Article
Times cited : (15)

References (48)
  • 1
    • 0035715945 scopus 로고    scopus 로고
    • Prolyl isomerases
    • Schmid, F. X. (2001) Prolyl isomerases. Adv. Protein Chem. 59, 243-282.
    • (2001) Adv. Protein Chem , vol.59 , pp. 243-282
    • Schmid, F.X.1
  • 2
    • 28444439801 scopus 로고    scopus 로고
    • Insights into the catalytic mechanism of peptidyl prolyl cis/trans isomerases
    • Fangḧanel, J., and Fischer, G. (2004) Insights into the catalytic mechanism of peptidyl prolyl cis/trans isomerases. Front. Biosci. 9, 3453-3478.
    • (2004) Front. Biosci , vol.9 , pp. 3453-3478
    • Fangḧanel, J.1    Fischer, G.2
  • 4
    • 0842266604 scopus 로고    scopus 로고
    • Oxidative protein folding in eukaryotes: Mechanisms and consequences
    • Tu, B. P., and Weissmann, J. S. (2004) Oxidative protein folding in eukaryotes: Mechanisms and consequences. J. Cell Biol. 164, 341-346.
    • (2004) J. Cell Biol , vol.164 , pp. 341-346
    • Tu, B.P.1    Weissmann, J.S.2
  • 5
  • 6
    • 0024959449 scopus 로고
    • Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins
    • Fischer, G., Wittmann-Liebold, B., Lang, K., Kiefhaber, T., and Schmid, F. X. (1989) Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins. Nature 337, 476-478.
    • (1989) Nature , vol.337 , pp. 476-478
    • Fischer, G.1    Wittmann-Liebold, B.2    Lang, K.3    Kiefhaber, T.4    Schmid, F.X.5
  • 7
    • 0024959451 scopus 로고
    • Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin
    • Takahashi, N., Hayano, T., and Suzuki, M. (1989) Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin. Nature 337, 473-475.
    • (1989) Nature , vol.337 , pp. 473-475
    • Takahashi, N.1    Hayano, T.2    Suzuki, M.3
  • 8
    • 0026499641 scopus 로고
    • Isomerase and chaperone activity of prolyl isomerase in the folding of carbonic anhydrase
    • Freskgå rd, P.-O., Bergenhem, N., Jonsson, B.-H., Svensson, M., and Carlsson, U. (1992) Isomerase and chaperone activity of prolyl isomerase in the folding of carbonic anhydrase. Science 258, 466-468.
    • (1992) Science , vol.258 , pp. 466-468
    • Freskgå rd, P.-O.1    Bergenhem, N.2    Jonsson, B.-H.3    Svensson, M.4    Carlsson, U.5
  • 9
    • 0028278089 scopus 로고
    • Reassessment of the putative chaperone function of prolyl-cis/transisomerases
    • Kern, G., Kern, D., Schmid, F. X., and Fischer, G. (1994) Reassessment of the putative chaperone function of prolyl-cis/transisomerases. FEBS Lett. 348, 145-148.
    • (1994) FEBS Lett , vol.348 , pp. 145-148
    • Kern, G.1    Kern, D.2    Schmid, F.X.3    Fischer, G.4
  • 10
    • 0028928739 scopus 로고
    • A kinetic analysis of the folding of human carbonic anhydrase II and its catalysis by cyclophilin
    • Kern, G., Kern, D., Schmid, F. X., and Fischer, G. (1995) A kinetic analysis of the folding of human carbonic anhydrase II and its catalysis by cyclophilin. J. Biol. Chem. 270, 740-745.
    • (1995) J. Biol. Chem , vol.270 , pp. 740-745
    • Kern, G.1    Kern, D.2    Schmid, F.X.3    Fischer, G.4
  • 11
    • 0029852803 scopus 로고    scopus 로고
    • Chaperone function of Hsp90-associated proteins
    • Bose, S., Weikl, T., B̈ugl, H., and Buchner, J. (1996) Chaperone function of Hsp90-associated proteins. Science 274, 1718-1720.
    • (1996) Science , vol.274 , pp. 1718-1720
    • Bose, S.1    Weikl, T.2    B̈ugl, H.3    Buchner, J.4
  • 12
    • 0029852712 scopus 로고    scopus 로고
    • Molecular chaperone machines: Chaperone activities of the cyclophilin Cyp-40 and the steroid aporeceptor-associated protein p23
    • Freeman, B. C., Toft, D. O., and Morimoto, R. (1996) Molecular chaperone machines: Chaperone activities of the cyclophilin Cyp-40 and the steroid aporeceptor-associated protein p23. Science 274, 1718-1720.
    • (1996) Science , vol.274 , pp. 1718-1720
    • Freeman, B.C.1    Toft, D.O.2    Morimoto, R.3
  • 13
    • 0034968225 scopus 로고    scopus 로고
    • Functional analysis of the Hsp90-associated human peptidyl prolyl cis/trans isomerases FKBP51, FKBP52 and Cyp40
    • Pirkl, F., and Buchner, J. (2001) Functional analysis of the Hsp90-associated human peptidyl prolyl cis/trans isomerases FKBP51, FKBP52 and Cyp40. J. Mol. Biol. 308, 795-806.
    • (2001) J. Mol. Biol , vol.308 , pp. 795-806
    • Pirkl, F.1    Buchner, J.2
  • 14
    • 0038831330 scopus 로고    scopus 로고
    • The periplasmic Escherichia coli peptidylprolyl cis,trans-isomerase FkpA. II. Isomerase-independent chaperone activity in vitro
    • Ramm, K., and Pl̈uckthun, A. (2000) The periplasmic Escherichia coli peptidylprolyl cis,trans-isomerase FkpA. II. Isomerase-independent chaperone activity in vitro. J. Biol. Chem. 275, 17106-17113.
    • (2000) J. Biol. Chem , vol.275 , pp. 17106-17113
    • Ramm, K.1    Pl̈uckthun, A.2
  • 15
    • 0035863210 scopus 로고    scopus 로고
    • The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity
    • Behrens, S., Maier, R., de Cock, H., Schmid, F. X., and Gross, C. A. (2001) The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity. EMBO J. 20, 285-294.
    • (2001) EMBO J , vol.20 , pp. 285-294
    • Behrens, S.1    Maier, R.2    de Cock, H.3    Schmid, F.X.4    Gross, C.A.5
  • 16
    • 0033918740 scopus 로고    scopus 로고
    • Assisted folding of D-glyceraldehyde-3-phosphate dehydrogenase by trigger factor
    • Huang, G. C., Li, Z. Y., Zhou, J. M., and Fischer, G. (2000) Assisted folding of D-glyceraldehyde-3-phosphate dehydrogenase by trigger factor. Protein Sci. 9, 1254-1261.
    • (2000) Protein Sci , vol.9 , pp. 1254-1261
    • Huang, G.C.1    Li, Z.Y.2    Zhou, J.M.3    Fischer, G.4
  • 17
    • 0347297339 scopus 로고    scopus 로고
    • Wheat FKBP73 functions in vitro as a molecular chaperone independently of its peptidyl prolyl cis-trans isomerase activity
    • Kurek, I., Pirkl, F., Fischer, E., Buchner, J., and Breiman, A. (2002) Wheat FKBP73 functions in vitro as a molecular chaperone independently of its peptidyl prolyl cis-trans isomerase activity. Planta 215, 119-126.
    • (2002) Planta , vol.215 , pp. 119-126
    • Kurek, I.1    Pirkl, F.2    Fischer, E.3    Buchner, J.4    Breiman, A.5
  • 18
    • 0036154244 scopus 로고    scopus 로고
    • FK506 binding protein from the hyperthermophilic archaeon Pyrococcus horikoshii suppresses the aggregation of proteins in Escherichia coli
    • Ideno, A., Furutani, M., Iba, Y., Kurosawa, Y., and Maruyama, T. (2002) FK506 binding protein from the hyperthermophilic archaeon Pyrococcus horikoshii suppresses the aggregation of proteins in Escherichia coli. Appl. Environ. Microbiol. 68, 464-469.
    • (2002) Appl. Environ. Microbiol , vol.68 , pp. 464-469
    • Ideno, A.1    Furutani, M.2    Iba, Y.3    Kurosawa, Y.4    Maruyama, T.5
  • 19
    • 0035878729 scopus 로고    scopus 로고
    • FK506-binding protein of the hyperthermophilic archaeum, Thermococcus sp. KS-1, a cold-shock-inducible peptidyl-prolyl cistrans isomerase with activities to trap and refold denatured proteins
    • Ideno, A., Yoshida, T., Iida, T., Furutani, M., and Maruyama, T. (2001) FK506-binding protein of the hyperthermophilic archaeum, Thermococcus sp. KS-1, a cold-shock-inducible peptidyl-prolyl cistrans isomerase with activities to trap and refold denatured proteins. Biochem. J. 357, 465-471.
    • (2001) Biochem. J , vol.357 , pp. 465-471
    • Ideno, A.1    Yoshida, T.2    Iida, T.3    Furutani, M.4    Maruyama, T.5
  • 20
    • 0034681154 scopus 로고    scopus 로고
    • FK506 Binding Protein from a thermophilic archaeon, Methanococcus thermolithotrophicus, has chaperone-like activity in vitro
    • Furutani, M., Ideno, A., Iida, T., and Maruyama, T. (2000) FK506 Binding Protein from a thermophilic archaeon, Methanococcus thermolithotrophicus, has chaperone-like activity in vitro. Biochemistry 39, 453-462.
    • (2000) Biochemistry , vol.39 , pp. 453-462
    • Furutani, M.1    Ideno, A.2    Iida, T.3    Maruyama, T.4
  • 21
    • 0037033042 scopus 로고    scopus 로고
    • A single-domain cyclophilin from Leishmania donovani reactivates soluble aggregates of adenosine kinase by isomerase-independent chaperone function
    • Chakraborty, A., Das, I., Datta, R., Sen, B., Bhattacharyya, D., Mandal, C., and Datta, A. K. (2002) A single-domain cyclophilin from Leishmania donovani reactivates soluble aggregates of adenosine kinase by isomerase-independent chaperone function. J. Biol. Chem. 277, 47451-47460.
    • (2002) J. Biol. Chem , vol.277 , pp. 47451-47460
    • Chakraborty, A.1    Das, I.2    Datta, R.3    Sen, B.4    Bhattacharyya, D.5    Mandal, C.6    Datta, A.K.7
  • 22
    • 30144446085 scopus 로고    scopus 로고
    • SlyD proteins from different species exhibt high prolyl isomerase and chaperone activities
    • Scholz, C., Eckert, B., Hagn, F., Schaarschidt, P., Balbach, J., and Schmid, F. X. (2006) SlyD proteins from different species exhibt high prolyl isomerase and chaperone activities. Biochemistry 45, 20-33.
    • (2006) Biochemistry , vol.45 , pp. 20-33
    • Scholz, C.1    Eckert, B.2    Hagn, F.3    Schaarschidt, P.4    Balbach, J.5    Schmid, F.X.6
  • 24
    • 0027062923 scopus 로고
    • Renaturation of citrate synthase: Influence of denaturant and folding assistants
    • Zhi, W., Landrmy, S. J., Gierasch, L. M., and Srere, P. A. (1992) Renaturation of citrate synthase: Influence of denaturant and folding assistants. Protein Sci. 1, 522-529.
    • (1992) Protein Sci , vol.1 , pp. 522-529
    • Zhi, W.1    Landrmy, S.J.2    Gierasch, L.M.3    Srere, P.A.4
  • 25
    • 0026047767 scopus 로고
    • Altering the mouth of a hydrophobic pocket. Structure and kinetics of human carbonic anhydrase II mutants at residue Val-121
    • Nair, S. K., Calderone, T. L., Christanson, D. W., and Fierke, C. (1991) Altering the mouth of a hydrophobic pocket. Structure and kinetics of human carbonic anhydrase II mutants at residue Val-121. J. Biol. Chem. 266, 17320-17325.
    • (1991) J. Biol. Chem , vol.266 , pp. 17320-17325
    • Nair, S.K.1    Calderone, T.L.2    Christanson, D.W.3    Fierke, C.4
  • 26
    • 0027071803 scopus 로고
    • Active site mutants of human cyclophilin A separate peptidyl-prolyl isomerase activity from cyclosporin A binding and calcineurin inhibition
    • Zydowsky, L. D., Etzkorn, F. A., Chang, H. Y., Ferguson, S. B., Stolz, L. A., Ho, S. I., and Walsh, C. T. (1992) Active site mutants of human cyclophilin A separate peptidyl-prolyl isomerase activity from cyclosporin A binding and calcineurin inhibition. Protein Sci. 1, 1092-1099.
    • (1992) Protein Sci , vol.1 , pp. 1092-1099
    • Zydowsky, L.D.1    Etzkorn, F.A.2    Chang, H.Y.3    Ferguson, S.B.4    Stolz, L.A.5    Ho, S.I.6    Walsh, C.T.7
  • 27
    • 0142183477 scopus 로고    scopus 로고
    • Why is carbonic anhydrase essential to Escherichia coli?
    • Merlin, C., Masters, M., McAteer, S., and Coulson, A. (2003) Why is carbonic anhydrase essential to Escherichia coli? J. Bacteriol. 185, 6415-6424.
    • (2003) J. Bacteriol , vol.185 , pp. 6415-6424
    • Merlin, C.1    Masters, M.2    McAteer, S.3    Coulson, A.4
  • 29
    • 0027389744 scopus 로고
    • Characterization of folding intermediates of human carbonic anhydrase II: Probing substructure by chemical labeling of SH groups introduced by site-directed mutagenesis
    • Mårtensson, L. G., Jonsson, B. H., Freskgård, P. O., Kihlgren, A., Svensson, M., and Carlsson, U. (1993) Characterization of folding intermediates of human carbonic anhydrase II: Probing substructure by chemical labeling of SH groups introduced by site-directed mutagenesis. Biochemistry 32, 224-231.
    • (1993) Biochemistry , vol.32 , pp. 224-231
    • Mårtensson, L.G.1    Jonsson, B.H.2    Freskgård, P.O.3    Kihlgren, A.4    Svensson, M.5    Carlsson, U.6
  • 30
    • 0037207131 scopus 로고    scopus 로고
    • Dramatic stabilization of the native state of human carbonic anhydrase II by an engineered disulfide bond
    • Mårtensson, L. G., Karlsson, M., and Carlsson, U. (2002) Dramatic stabilization of the native state of human carbonic anhydrase II by an engineered disulfide bond. Biochemistry 41, 15867-15875.
    • (2002) Biochemistry , vol.41 , pp. 15867-15875
    • Mårtensson, L.G.1    Karlsson, M.2    Carlsson, U.3
  • 31
    • 0030848403 scopus 로고    scopus 로고
    • Cyclophilin active site mutants have native prolyl isomerase activity with a protein substrate
    • Scholz, C., Schindler, T., Dolinski, K., Heitman, J., and Schmid, F. X. (1997) Cyclophilin active site mutants have native prolyl isomerase activity with a protein substrate. FEBS Lett. 414, 69-73.
    • (1997) FEBS Lett , vol.414 , pp. 69-73
    • Scholz, C.1    Schindler, T.2    Dolinski, K.3    Heitman, J.4    Schmid, F.X.5
  • 32
    • 0015878753 scopus 로고
    • Denaturation and reactivation of human carbonic anhydrases in guanidine hydrochloride and urea
    • Carlsson, U., Henderson, L. E., and Lindskog, S. (1973) Denaturation and reactivation of human carbonic anhydrases in guanidine hydrochloride and urea. Biochim. Biophys. Acta 310, 376-387.
    • (1973) Biochim. Biophys. Acta , vol.310 , pp. 376-387
    • Carlsson, U.1    Henderson, L.E.2    Lindskog, S.3
  • 33
    • 38849183444 scopus 로고    scopus 로고
    • Thermodynamic interrogation of a folding disease: Mutant mapping of position 107 in human carbonic anhydrase II linked to marble brain disease
    • Almstedt, K., Mårtensson, L.-G., Carlsson, U., and Hammarstr̈om, P. (2008) Thermodynamic interrogation of a folding disease: Mutant mapping of position 107 in human carbonic anhydrase II linked to marble brain disease. Biochemistry 47, 1288-1298.
    • (2008) Biochemistry , vol.47 , pp. 1288-1298
    • Almstedt, K.1    Mårtensson, L.-G.2    Carlsson, U.3    Hammarstr̈om, P.4
  • 35
    • 18144400877 scopus 로고    scopus 로고
    • Efficient refolding of aggregation-prone citrate synthase by polyol osmolytes: How well are protein folding and stability aspects coupled?
    • Mishra, R., Seckler, R., and Bhat, R. (2005) Efficient refolding of aggregation-prone citrate synthase by polyol osmolytes: How well are protein folding and stability aspects coupled? J. Biol. Chem. 280, 15553-15560.
    • (2005) J. Biol. Chem , vol.280 , pp. 15553-15560
    • Mishra, R.1    Seckler, R.2    Bhat, R.3
  • 36
    • 0001647511 scopus 로고
    • The citrate-condensing enzyme of pigeon breast muscle and moth flight muscle
    • Srere, P. A., Brazil, H., and Gonen, L. (1963) The citrate-condensing enzyme of pigeon breast muscle and moth flight muscle. Acta Chem. Scand. 17, S129-S134.
    • (1963) Acta Chem. Scand , vol.17
    • Srere, P.A.1    Brazil, H.2    Gonen, L.3
  • 37
    • 4344710278 scopus 로고    scopus 로고
    • Unfolding a folding disease: Folding, misfolding and aggregation of the marble brain syndrome-associated mutant H107Y of human carbonic anhydrase II
    • Almstedt, K., Lundqvist, M., Carlsson, J., Karlsson, M., Persson, B., Jonsson, B.-H., Carlsson, U., and Hammarstr̈om, P. (2004) Unfolding a folding disease: Folding, misfolding and aggregation of the marble brain syndrome-associated mutant H107Y of human carbonic anhydrase II. J. Mol. Biol. 342, 619-633.
    • (2004) J. Mol. Biol , vol.342 , pp. 619-633
    • Almstedt, K.1    Lundqvist, M.2    Carlsson, J.3    Karlsson, M.4    Persson, B.5    Jonsson, B.-H.6    Carlsson, U.7    Hammarstr̈om, P.8
  • 38
  • 39
    • 0033524418 scopus 로고    scopus 로고
    • EPR mapping of interactions between spin-labeled variants of human carbonic anhydrase II and GroEL. Evidence for increased flexibility of the hydrophobic core by the interaction
    • Persson, M., Lindgren, M., Hammarstr̈om, P., Svensson, M., Jonsson, B.-H., and Carlsson, U. (1999) EPR mapping of interactions between spin-labeled variants of human carbonic anhydrase II and GroEL. Evidence for increased flexibility of the hydrophobic core by the interaction. Biochemistry 38, 432-441.
    • (1999) Biochemistry , vol.38 , pp. 432-441
    • Persson, M.1    Lindgren, M.2    Hammarstr̈om, P.3    Svensson, M.4    Jonsson, B.-H.5    Carlsson, U.6
  • 40
    • 0035877704 scopus 로고    scopus 로고
    • Protein compactness measured by FRET: Human carbonic anhydrase II is considerably expanded by the interaction of GroEL
    • Hammarstr̈om, P., Persson, M., and Carlsson, U. (2001) Protein compactness measured by FRET: Human carbonic anhydrase II is considerably expanded by the interaction of GroEL. J. Biol. Chem. 276, 21765-21775.
    • (2001) J. Biol. Chem , vol.276 , pp. 21765-21775
    • Hammarstr̈om, P.1    Persson, M.2    Carlsson, U.3
  • 41
    • 59949105375 scopus 로고    scopus 로고
    • A Nonessential Role for Arg 55 in Cyclophilin 18 for Catalysis of Proline Isomerization during Protein Folding
    • Moparthi, S. B., Hammarstr̈om, P., and Carlsson, U. (2009) A Nonessential Role for Arg 55 in Cyclophilin 18 for Catalysis of Proline Isomerization during Protein Folding. Protein Sci. 18, 475-479.
    • (2009) Protein Sci , vol.18 , pp. 475-479
    • Moparthi, S.B.1    Hammarstr̈om, P.2    Carlsson, U.3
  • 42
    • 0343907904 scopus 로고    scopus 로고
    • Formation of local asymmetric structures in the slow folding reaction of human carbonic anhydrase II
    • Andersson, D., Freskgård, P.-O., Jonsson, B.-H., and Carlsson, U. (1997) Formation of local asymmetric structures in the slow folding reaction of human carbonic anhydrase II. Biochemistry 36, 4623-4630.
    • (1997) Biochemistry , vol.36 , pp. 4623-4630
    • Andersson, D.1    Freskgård, P.-O.2    Jonsson, B.-H.3    Carlsson, U.4
  • 43
    • 0036929926 scopus 로고    scopus 로고
    • Evaluation of similarities in the cis/trans isomerase function of trigger factor and DnaK
    • Schiene-Fischer, C., Habazetti, J., Tradler, T., and Fischer, G. (2002) Evaluation of similarities in the cis/trans isomerase function of trigger factor and DnaK. Biol. Chem. 383, 1865-1873.
    • (2002) Biol. Chem , vol.383 , pp. 1865-1873
    • Schiene-Fischer, C.1    Habazetti, J.2    Tradler, T.3    Fischer, G.4
  • 45
    • 2542540688 scopus 로고    scopus 로고
    • Circumnavigating misfolding traps in the energy landscape through protein engineering: Suppression of molten globule and aggregation in carbonic anhydrase
    • Karlsson, M., Mårtensson, L.-G., Olofsson, P., and Carlsson, U. (2004) Circumnavigating misfolding traps in the energy landscape through protein engineering: Suppression of molten globule and aggregation in carbonic anhydrase. Biochemistry 43, 6803-6807.
    • (2004) Biochemistry , vol.43 , pp. 6803-6807
    • Karlsson, M.1    Mårtensson, L.-G.2    Olofsson, P.3    Carlsson, U.4
  • 47
    • 0027772159 scopus 로고
    • X-ray structure of a monomeric cyclophilin A-cyclosporin A crystal complex at 2.1 Å resolution
    • Mikol, V., Kallen, J., Pfl̈ugl, G., and Walkinshaw, M. D. (1993) X-ray structure of a monomeric cyclophilin A-cyclosporin A crystal complex at 2.1 Å resolution. J. Mol. Biol. 234, 1119-1130.
    • (1993) J. Mol. Biol , vol.234 , pp. 1119-1130
    • Mikol, V.1    Kallen, J.2    Pfl̈ugl, G.3    Walkinshaw, M.D.4
  • 48
    • 0034774703 scopus 로고    scopus 로고
    • Chaperonelike activity of peptidyl-prolyl cis-trans isomerase during creatin kinase refolding
    • Ou, W.-B., Wei, L., Park, Y.-D., and Zhou, H.-M. (2001) Chaperonelike activity of peptidyl-prolyl cis-trans isomerase during creatin kinase refolding. Protein Sci. 10, 2346-2355.
    • (2001) Protein Sci , vol.10 , pp. 2346-2355
    • Ou, W.-B.1    Wei, L.2    Park, Y.-D.3    Zhou, H.-M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.