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Volumn 10, Issue 1, 1996, Pages 84-92

Stability and folding of ultrastable proteins: Eye lens crystallins and enzymes from thermophiles

Author keywords

chaperones; domains; linkers; oligomeric protein; protein stability

Indexed keywords

CHAPERONIN; CRYSTALLIN; ENOLASE; LACTATE DEHYDROGENASE; PHOSPHOGLYCERATE KINASE; TRIOSEPHOSPHATE ISOMERASE;

EID: 0030067190     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fasebj.10.1.8566552     Document Type: Review
Times cited : (99)

References (50)
  • 1
    • 0026320508 scopus 로고
    • Protein stability and molecular adaptation to extreme conditions
    • Jaenicke, R. (1991) Protein stability and molecular adaptation to extreme conditions. Eur. J. Biochem. 202, 715-728
    • (1991) Eur. J. Biochem. , vol.202 , pp. 715-728
    • Jaenicke, R.1
  • 2
    • 77956856574 scopus 로고
    • Biochemistry of archaea
    • (Kates, M., Kushner, D. J., and Metheson, A. T., eds) Elsevier, Amsterdam, Holland
    • Woese, C. R. (1993) Biochemistry of archaea. In New Comprehensive Biochemistry (Kates, M., Kushner, D. J., and Metheson, A. T., eds) Vol. 26, pp. VII-XXIX, Elsevier, Amsterdam, Holland
    • (1993) New Comprehensive Biochemistry , vol.26
    • Woese, C.R.1
  • 3
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill, K. A. (1990) Dominant forces in protein folding. Biochemistry 29, 7133-7155
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.A.1
  • 4
    • 0029685460 scopus 로고
    • Protein folding and association: Significance of in vitro studies for self-organization and targeting in the cell
    • In press
    • Jaenicke, R. (1995) Protein folding and association: significance of in vitro studies for self-organization and targeting in the cell. Curr. Top. Cell. Regul. 34 In press
    • (1995) Curr. Top. Cell. Regul. , vol.34
    • Jaenicke, R.1
  • 5
    • 0019363271 scopus 로고
    • Enzymes under extremes of physical conditions
    • Jaenicke, R. (1981) Enzymes under extremes of physical conditions. Annu. Rev. Biophys. Bioeng. 10, 1-67
    • (1981) Annu. Rev. Biophys. Bioeng. , vol.10 , pp. 1-67
    • Jaenicke, R.1
  • 6
    • 0026583113 scopus 로고
    • Adaptations to high hydrostatic pressure
    • Somero, G. N. (1992) Adaptations to high hydrostatic pressure. Annu. Rev. Physiol. 54, 557-577
    • (1992) Annu. Rev. Physiol. , vol.54 , pp. 557-577
    • Somero, G.N.1
  • 7
    • 0025876740 scopus 로고
    • Protein Folding: Local structures, domains, subunits, and assemblies
    • Jaenicke, R. (1991) Protein Folding: Local structures, domains, subunits, and assemblies. Biochemistry 30, 3147-3161
    • (1991) Biochemistry , vol.30 , pp. 3147-3161
    • Jaenicke, R.1
  • 8
    • 0026700861 scopus 로고
    • Protein folding and protein refolding
    • Seckler, R., and Jaenicke, R. (1992) Protein folding and protein refolding FASEB J. 6, 2545-2552
    • (1992) FASEB J. , vol.6 , pp. 2545-2552
    • Seckler, R.1    Jaenicke, R.2
  • 9
    • 0029249945 scopus 로고
    • The nature of protein folding pathways: The classical versus the new view
    • Baldwin, R. L. (1995) The nature of protein folding pathways: the classical versus the new view. J. Biomol. NMR 5, 103-109
    • (1995) J. Biomol. NMR , vol.5 , pp. 103-109
    • Baldwin, R.L.1
  • 12
    • 0024063265 scopus 로고
    • On the relevance of non-random polypeptide conformations for protein folding
    • Creighton, T. E. (1988) On the relevance of non-random polypeptide conformations for protein folding. Biophys. Chem. 311, 155-1162
    • (1988) Biophys. Chem. , vol.311 , pp. 155-1162
    • Creighton, T.E.1
  • 15
    • 0025339471 scopus 로고
    • Folding of an all-β protein: Independent domain folding in γII-crystallin from calf eye lens
    • Rudolph, R., Siebendritt, R., Nesslauer, G., Sharma, A. K., and Jaenicke, R. (1990) Folding of an all-β protein: Independent domain folding in γII-crystallin from calf eye lens. Proc. Natl Acad. Sci. USA 87, 4625-4629
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 4625-4629
    • Rudolph, R.1    Siebendritt, R.2    Nesslauer, G.3    Sharma, A.K.4    Jaenicke, R.5
  • 16
    • 0023506457 scopus 로고
    • Folding and association of proteins
    • Jaenicke, R. (1987) Folding and association of proteins. Progr. Biophys. Mol. Biol. 49, 117-237
    • (1987) Progr. Biophys. Mol. Biol. , vol.49 , pp. 117-237
    • Jaenicke, R.1
  • 18
    • 0028204771 scopus 로고
    • Domain swapping: Entangling alliances between proteins
    • Bennett, M. J., Cho, S., and Eisenberg, D. (1994) Domain swapping: Entangling alliances between proteins. Proc. Natl Acad. Sci. USA 91, 3127-3131
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 3127-3131
    • Bennett, M.J.1    Cho, S.2    Eisenberg, D.3
  • 19
    • 0028053274 scopus 로고
    • Domain interactions and connecting peptides in lens crystallins
    • Mayr, E.-M., Jaenicke, R., and Glockshuber, R. (1994) Domain interactions and connecting peptides in lens crystallins J. Mol. Biol. 235, 84-88
    • (1994) J. Mol. Biol. , vol.235 , pp. 84-88
    • Mayr, E.-M.1    Jaenicke, R.2    Glockshuber, R.3
  • 20
    • 0028171466 scopus 로고
    • Dimerization of βB2-crystallin: The role of the connecting peptide and the N- and C-terminal extensions
    • Trinkl, S., Glockshuber, R., and Jaenicke, R. (1994) Dimerization of βB2-crystallin: The role of the connecting peptide and the N- and C-terminal extensions. Protein Sci. 3, 1392-1400
    • (1994) Protein Sci. , vol.3 , pp. 1392-1400
    • Trinkl, S.1    Glockshuber, R.2    Jaenicke, R.3
  • 21
    • 0023131203 scopus 로고
    • Proteolytic dimers of porcine LDH: Characterization, folding and reconstitution of the truncated and nicked polypeptide chain
    • Opitz, U., Rudolph, R., Jaenicke, R., Ericsson, L., and Neurath, H. (1987) Proteolytic dimers of porcine LDH: Characterization, folding and reconstitution of the truncated and nicked polypeptide chain. Biochemistry 26, 1399-1406
    • (1987) Biochemistry , vol.26 , pp. 1399-1406
    • Opitz, U.1    Rudolph, R.2    Jaenicke, R.3    Ericsson, L.4    Neurath, H.5
  • 22
    • 0025843479 scopus 로고
    • A kinetic study of the competition between renaturation and aggregation during the refolding of denatured reduced egg-white lysozyme
    • Goldberg, M. E., Rudolph, R., and Jaenicke, R. (1991) A kinetic study of the competition between renaturation and aggregation during the refolding of denatured reduced egg-white lysozyme. Biochemistry 30, 2790-2797
    • (1991) Biochemistry , vol.30 , pp. 2790-2797
    • Goldberg, M.E.1    Rudolph, R.2    Jaenicke, R.3
  • 24
    • 0009371409 scopus 로고
    • Protein folding: From "unboiling an egg" to "catalysis of folding"
    • Jaenicke, R., and Buchner, J. (1993) Protein folding: From "unboiling an egg" to "catalysis of folding" Chemtracts: Biochem. Mol. Biol. 4, 1-30
    • (1993) Chemtracts: Biochem. Mol. Biol. , vol.4 , pp. 1-30
    • Jaenicke, R.1    Buchner, J.2
  • 25
    • 0029653845 scopus 로고
    • Folding and association versus misfolding and aggregation of proteins
    • Jaenicke, R. (1995) Folding and association versus misfolding and aggregation of proteins. Philos. Trans. R. Soc. Lond. 348, 97-105
    • (1995) Philos. Trans. R. Soc. Lond. , vol.348 , pp. 97-105
    • Jaenicke, R.1
  • 26
    • 0025892424 scopus 로고
    • A novel ATPase complex selectively accumulated upon heat shock is a major cellular component of thermophilic archaebacteria
    • Phipps, B. M., Hofmann, A., Steuer, K. O., and Baumeister, W. (1991) A novel ATPase complex selectively accumulated upon heat shock is a major cellular component of thermophilic archaebacteria. EMBO J, 10, 1711-1722
    • (1991) EMBO J , vol.10 , pp. 1711-1722
    • Phipps, B.M.1    Hofmann, A.2    Steuer, K.O.3    Baumeister, W.4
  • 27
    • 0001912876 scopus 로고
    • Thermoadaptation of methanogenic bacteria by intracellular ion concentration
    • Hensel, R., and König, H. (1988) Thermoadaptation of methanogenic bacteria by intracellular ion concentration. FEMS Microbiol. Lett. 49, 75-79.
    • (1988) FEMS Microbiol. Lett. , vol.49 , pp. 75-79
    • Hensel, R.1    König, H.2
  • 28
    • 0024856531 scopus 로고
    • A novel group of abyssal methanogenic archaea growing at 110°C
    • Huber, R., Kurr, M., Jannasch, H. W., and Stettcr, K. O. (1989) A novel group of abyssal methanogenic archaea growing at 110°C. Nature (London) 342, 833-834
    • (1989) Nature (London) , vol.342 , pp. 833-834
    • Huber, R.1    Kurr, M.2    Jannasch, H.W.3    Stettcr, K.O.4
  • 29
    • 0027069576 scopus 로고
    • Stability and characterization of the stabilizing effect of point mutations of pyruvate oxidase from Lact. plantarum
    • Risse, B., Stempfer, G., Rudolph, R., and Jaenicke, R. (1992) Stability and characterization of the stabilizing effect of point mutations of pyruvate oxidase from Lact. plantarum. Protein Sci. 1, 1699-1718
    • (1992) Protein Sci. , vol.1 , pp. 1699-1718
    • Risse, B.1    Stempfer, G.2    Rudolph, R.3    Jaenicke, R.4
  • 30
    • 0027050823 scopus 로고
    • Quaternary structure and stability of internal, external and core-glycosylated invertase from yeast
    • Kern, G., Schülke, N., Schmid, F. X., and Jaenicke, R. (1992) Quaternary structure and stability of internal, external and core-glycosylated invertase from yeast. Protein Sci 1, 120-131
    • (1992) Protein Sci , vol.1 , pp. 120-131
    • Kern, G.1    Schülke, N.2    Schmid, F.X.3    Jaenicke, R.4
  • 31
    • 0027507503 scopus 로고
    • Kinetics of folding and association of differently glycosylated variants of mvertase from Sacch. cerevisiae
    • Kern, G., Kern, D., Jaenicke, R., and Seckler, R. (1993) Kinetics of folding and association of differently glycosylated variants of mvertase from Sacch. cerevisiae. Protein Sci. 2, 1862-1868
    • (1993) Protein Sci. , vol.2 , pp. 1862-1868
    • Kern, G.1    Kern, D.2    Jaenicke, R.3    Seckler, R.4
  • 32
    • 0026648514 scopus 로고
    • Stability and reconstitution of GAPDH from the hyperthermophilic eubacterium Tm
    • Rehaber, V., and Jaenicke, R. (1992) Stability and reconstitution of GAPDH from the hyperthermophilic eubacterium Tm. J. Biol. Chem. 267, 10999-11006
    • (1992) J. Biol. Chem. , vol.267 , pp. 10999-11006
    • Rehaber, V.1    Jaenicke, R.2
  • 33
    • 0025879614 scopus 로고
    • Folding intermediates of hyperthermophilic GAPDH from Tm are trapped at low temperature
    • Schultes, V., and Jaenicke, R. (1991) Folding intermediates of hyperthermophilic GAPDH from Tm are trapped at low temperature. FEBS Lett. 290,235-238.
    • (1991) FEBS Lett. , vol.290 , pp. 235-238
    • Schultes, V.1    Jaenicke, R.2
  • 36
    • 0021753827 scopus 로고
    • Hydrolytic stability of biomolecules at high temperatures and its implication for life at 250°C
    • White, R. H. (1984) Hydrolytic stability of biomolecules at high temperatures and its implication for life at 250°C. Nature (London) 310, 430-432
    • (1984) Nature (London) , vol.310 , pp. 430-432
    • White, R.H.1
  • 37
    • 0000180763 scopus 로고
    • Temperature dependence of hydiophobic interactions in protein folding
    • Baldwin, R. L. (1986) Temperature dependence of hydiophobic interactions in protein folding. Proc. Natl. Acad. Sci. USA 83, 8069-6072
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 8069-16072
    • Baldwin, R.L.1
  • 38
    • 0002693020 scopus 로고
    • Physical basis of the stability of the folded conformations of proteins
    • (Creighton, T. E., ed) Freeman, New York
    • Privalov, P. L. (1992) Physical basis of the stability of the folded conformations of proteins. In Protein Folding (Creighton, T. E., ed) pp. 83-126, Freeman, New York
    • (1992) Protein Folding , pp. 83-126
    • Privalov, P.L.1
  • 39
    • 0028014604 scopus 로고
    • On the relevance of sequence statistics for the properties of extremophilic proteins
    • Böhm, G., and Jaenicke, R. (1994) On the relevance of sequence statistics for the properties of extremophilic proteins. Int. J. Pept. Protein Res. 43, 97-106
    • (1994) Int. J. Pept. Protein Res. , vol.43 , pp. 97-106
    • Böhm, G.1    Jaenicke, R.2
  • 40
    • 0028968018 scopus 로고
    • Studies on protein stability with T4 lysozyme
    • Matthews, B. W. (1995) Studies on protein stability with T4 lysozyme. Adv. Prot. Chem. 46, 249-278
    • (1995) Adv. Prot. Chem. , vol.46 , pp. 249-278
    • Matthews, B.W.1
  • 42
    • 0028819196 scopus 로고
    • PGK and TIM from the hyperthermophilic bacterium Tm form a covalent bifunctional enzyme complex
    • Schung, H., Beaucamp, N., Ostendorp, R., Jaenicke, R., Adler, E., and Knowles, J. (1995) PGK and TIM from the hyperthermophilic bacterium Tm form a covalent bifunctional enzyme complex. EMBO J. 14, 442-451
    • (1995) EMBO J. , vol.14 , pp. 442-451
    • Schung, H.1    Beaucamp, N.2    Ostendorp, R.3    Jaenicke, R.4    Adler, E.5    Knowles, J.6
  • 43
    • 0027318085 scopus 로고
    • Cloning and expression of GAPDH from the hyperthermophilic bacterium Tm
    • Tomschy, A., Glockshuber, R., and Jaenieke, R. (1993) Cloning and expression of GAPDH from the hyperthermophilic bacterium Tm. Eur. J. Biochem. 214, 43-50
    • (1993) Eur. J. Biochem. , vol.214 , pp. 43-50
    • Tomschy, A.1    Glockshuber, R.2    Jaenieke, R.3
  • 44
    • 0028903461 scopus 로고
    • The crystal structure of holo-GAPDH from the hyperthermophilic bacterium Tm at 2.5 a resolution
    • Korndörfer, I., Steipe, B., Huber, R., Tomsehy, A., and Jaenicke, R. (1995) The crystal structure of holo-GAPDH from the hyperthermophilic bacterium Tm at 2.5 A resolution. J. Mol. Biol. 246, 511-521
    • (1995) J. Mol. Biol. , vol.246 , pp. 511-521
    • Korndörfer, I.1    Steipe, B.2    Huber, R.3    Tomsehy, A.4    Jaenicke, R.5
  • 45
    • 0028912631 scopus 로고
    • Octameric enolase from the hyperthermophilic bacterium Tm: Purification, characterization and image processing
    • Schurig, H., Rutkat, K., Rachel, R., and Jaenicke, R. (1995) Octameric enolase from the hyperthermophilic bacterium Tm: Purification, characterization and image processing. Protein Sci. 4, 228-236
    • (1995) Protein Sci. , vol.4 , pp. 228-236
    • Schurig, H.1    Rutkat, K.2    Rachel, R.3    Jaenicke, R.4
  • 46
    • 0025093446 scopus 로고
    • LDH from the extreme thermophilic eubacterium Tm
    • Wrba, A., Jaenicke, R., Huber, R., and Stetter, K. O. (1990) LDH from the extreme thermophilic eubacterium Tm. Eur. J. Biochem. 188, 195-201
    • (1990) Eur. J. Biochem. , vol.188 , pp. 195-201
    • Wrba, A.1    Jaenicke, R.2    Huber, R.3    Stetter, K.O.4
  • 47
    • 0027524560 scopus 로고
    • The L-LDH gene of the hyperthermophilic bacterium Tm cloned by complementation in E. coli
    • Ostendorp, R., Liebl, W., Schurig, H., and Jaenicke, R. (1993) The L-LDH gene of the hyperthermophilic bacterium Tm cloned by complementation in E. coli. Eur. J. Biochem. 216, 709-715
    • (1993) Eur. J. Biochem. , vol.216 , pp. 709-715
    • Ostendorp, R.1    Liebl, W.2    Schurig, H.3    Jaenicke, R.4
  • 48
    • 0024970964 scopus 로고
    • Catalytic properties of thermophilic LDH and halophilic MDH at high temperatures and low water activity. Eur
    • Hecht, K., Wrba, A., and Jaenicke, R. (1990) Catalytic properties of thermophilic LDH and halophilic MDH at high temperatures and low water activity. Eur. J. Biochem. 183, 69-74
    • (1990) J. Biochem. , vol.183 , pp. 69-74
    • Hecht, K.1    Wrba, A.2    Jaenicke, R.3
  • 49
    • 0027488713 scopus 로고
    • Stabilization of creatinase from Ps. putida by random mutagenesis
    • Schumann, J., Böhm, G., Schumacher, G., Rudolph, R., and Jaenicke, R. (1993) Stabilization of creatinase from Ps. putida by random mutagenesis. Protein Sci. 2, 1612-1620
    • (1993) Protein Sci. , vol.2 , pp. 1612-1620
    • Schumann, J.1    Böhm, G.2    Schumacher, G.3    Rudolph, R.4    Jaenicke, R.5
  • 50


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