The recombinant thermosome from the hyperthermophilic archaeon Methanopyrus kandleri: In vitro analysis of its chaperone activity

Biological Chemistry

Volumn 380, Issue 1, 1999, Pages 55-62

  Minuth, Torsten ^a   Henn, Martina ^a   Rutkat, Kerstin ^a   Andrä, Stefan ^a   Frey, Gerhard ^a   Rachel, Reinhard ^a   Stetter, Karl Otto ^a   Jaenicke, Rainer ^a  

^a UNIVERSITY OF REGENSBURG   (Germany)

Author keywords

Chaperonin; Hyperthermophilic methanogen; Methanopyrus kandleri; Protein aggregation; Thermosome

Indexed keywords

ALCOHOL DEHYDROGENASE; ALPHA GLUCOSIDASE; BACTERIAL PROTEIN; BOVINE INSULIN; CHAPERONIN; CITRATE SYNTHASE; PHOSPHOGLYCERATE KINASE; RECOMBINANT PROTEIN; THERMOSOME; UNCLASSIFIED DRUG;

ARCHAEBACTERIUM; ARTICLE; COMPLEX FORMATION; ENZYME SUBSTRATE; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; SWINE; THERMOPHILIC BACTERIUM; YEAST;

ALCOHOL DEHYDROGENASE; ALPHA-GLUCOSIDASES; ANIMALS; ARCHAEAL PROTEINS; CATTLE; CHAPERONINS; CHEMISTRY, PHYSICAL; CITRATE (SI)-SYNTHASE; ENZYME ACTIVATION; EURYARCHAEOTA; INSULIN; INSULIN ANTAGONISTS; PHOSPHOGLYCERATE KINASE; RECOMBINANT PROTEINS; SWINE;

ARCHAEA; BACTERIA (MICROORGANISMS); BOVINAE; ESCHERICHIA COLI; METHANOPYRUS KANDLERI; SUS SCROFA; THERMOTOGA;

EID: 0032930104     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/BC.1999.007     Document Type: Article

References (41)

1. Andrä, S., Frey, G., Nitsch, M., Baumeister, W., and Stetter, K.O. (1996). Purification and structural characterization of the thermosome from the hyperthermophilic archaeum Methanopyrus kandleri. FEBS Letters 379, 127-131.
2. +-dependent ATPase activity. Eur. J. Biochem. 255, 93-99.
3. Beissinger, M., and Buchner, J. (1998). How chaperonesfold proteins. Biol. Chem. 379, 245-259.
4. Bergmeyer, H.U. (ed.) (1983). Alcoholdehydrogenase. In: Methods in Enzymatic Analysis, Vol. 2, 3rd. Ed. (Weinheim, Germany: Verlag Chemie), 139-141.
5. Blum, H., Beier, H., and Gross, H.J. (1987). Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels. Electrophoresis 8, 93-99.
6. M) and thermostability in the presence of salts. Arch. Microbiol. 156, 517-524.
7. Breitung, J., Börner, G., Scholz, S., Lindner, D., Stetter, K.O., and Thauer, R.K. (1992). Salt dependence, kinetic properties and catalytic mechanism of N-formyltransferase from the extreme thermophile Methanopyuss kandleri. Eur. J. Biochem. 270, 971-981.
8. Buchner, J., Schmidt, M., Fuchs, M., Jaenicke, R., Rudolph, R., Schmid, F.X., and Kiefhaber, T. (1991). GroE facilitates refolding of citrate synthase by suppressing aggregation. Biochemistry 30, 1586-1591.
9. Bukau, B., and Norwich, A.L. (1998). The Hsp70 and Hsp60 chaperone machines. Cell 92, 351-366.
10. Dams, T., Ostendorp, R., Ott, M., Rutkat, K., and Jaenicke, R. (1996). Tetrameric and octameric lactate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima: Structure and stability of the two active forms. Eur. J. Biochem. 240, 274-279.
11. Daniel, R.M., Dines, M., and Petach, H.H. (1996). The denaturation and degradation of stable enzymes at high temperatures. Biochem. J. 317, 1-11.
12. Ditzel, L., Löwe, J., Stock, D., Stetter, K.O., Huber, H., Huber, R., and Steinbacher, S. (1998). Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT. Cell 93, 125-138.
13. Ehrnsperger, M., Gräber, S., Gaestel, M., and Buchner, J. (1997). Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation. EMBO J. 16, 221-229.
14. Ermler, U., Merckel, M.C., Thauer, R.K., and Shima, S. (1997). Formylmethanofuran:tetrahydromethanopterin formyltransferase from Methanopyrus kandleri-new insights into salt dependence and thermostability. Structure 5, 635-645.
15. Fairbanks, G., Steck, T.L., and Wallach, D.F.H. (1971). Electrophoretic analysis of the major polypeptides of the human erythrocytemembrane. Biochemistry 70, 2606-2617.
16. Fenton, W.A., and Norwich, A.L. (1997). GroEL-mediated protein folding. Prot. Sci. 6, 743-760.
17. Fink, A.L., and Goto, Y. (1998). Molecular Chaperones in the Life Cycle of Proteins (New York, NY: Marcel Dekker, Inc.).
18. Fling, S., and Gregerson, D.S. (1986). Peptide and protein molecular weight determination by electrophoresis, using a high-molarity Tris-buffer system without urea. Anal. Biochem. 155, 83-88.
19. Guagliardi, A., Cerchia, L., Bartolucci, S., and Rossi, M. (1994). The chaperonin from the archaeon Sulfolobus solfataricus promotes correct refolding and prevents thermal denaturation in vitro. Protein Sciences, 1436-1443.
20. Guagliardi, A., Cerchia, L., and Rossi, M. (1995). Prevention of in vitro protein thermal aggregation by the Sulfolobus solfataricus chaperonin. J. Biol. Chem. 270, 28126-28132.
21. Hendrick, J.P., and Hartl, F.U. (1993). Molecular chaperone functions of heat shock proteins Annu. Rev. Biochem. 62, 349-384.
22. Hoffmann, A. (1992). Reinigung, Charakterisierung und partielle Sequenzierung einer ATPase aus dem hyperthermophilen Archaeon Pyrodictium occultum, Ph.D. Thesis, University of Regensburg.
23. Horovitz, A. (1998). Structural aspects of GroEL function. Current Opinion in Structural Biology 8, 93-100.
24. Jaenicke, R. (1991). Protein stability and molecular adaptation to extreme conditions. Eur. J. Biochem. 202, 715-728.
25. Jaenicke, R., and Seckler, R. (1997). Protein misassembly in vitro. Adv. Protein Chem. 50, 1-59.
26. Klumpp, M., Baumeister, W., and Essen, L.O. (1997). Structure of the substrate binding domain of the thermosome, an archaeal group II chaperonin. Cell 91, 263-270.
27. Lindner, P. (1996). Untersuchungen zur Expression der Thermosom-Gene von Methanopyrus kandleri und Pyrodictium occultum. Diploma Thesis, University of Regensburg.
28. Nakamura, N., Taguchi, H., Ishii, N., Yoshida, M., Suzuki, M., Endo, I., Miura, K., and Yohda, M. (1997). Purification and molecular cloning of the group II chaperonin from acidothermophilic archaeon, Sulfolobus Sp. Strain 7. BBRC 236, 727-732.
29. Pace, C.N., Vajdos, F., Fee, L., Grimsley, G., and Gray, T. (1995). How to measure and predict the molar absorption coefficient of a protein. Protein Science 4, 2411-2423.
30. Phipps, B.M., Hoffmann, A., Stetter, K.O., and Baumeister, W. (1991). A novel ATPase complex selectively accumulated upon heat shock is a major cellular component of thermophilic archaebacteria. The EMBO J. 10, 1711-1722.
31. Quaite-Randall, E., Trent, J.D., Josephs, R., and Joachimiak, A. (1995). Conformational cycle of the archaeosome, a TCP1-like chaperonin from Sulfolobus shibatae. J. Biol. Chem. 270, 28818-28823.
32. Sanger, F. (1949). Fractionation of oxidized insulin. Biochem. J. 44, 126-128.
33. Schmidt, M. (1991). Strukturelle und funktionelle Charakterisierung von GroE. Diploma Thesis, University of Regensburg.
34. Schurig, H. (1995). Untersuchungen zur Struktur und Funktion von thermostabilen Proteinen: Triosephosphat-Isomerase, Phosphoglycerat-Kinase und Enolase aus dem hyperthermophilen Bakterium Thermotoga maritima. PhD Thesis, University of Regensburg.
35. Sparrer, H. (1992). Strukturelle und funktionelle Charakterisierung von PL-19 ATPase aus Pyrodictium occultum. Diploma Thesis, University of Regensburg.
36. Trent, J.D., Nimmesgern, E., Wall, J.S., Hartl, U., and Norwich, A.L. (1991). A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1. Nature 354, 490-493.
37. Waldmann, T., Nimmesgern, E., Nitsch, M., Peters, J., Pfeifer, G., Müller, S., Kellermann, J., Engel., A., Hartl., F.U., and Baumeister, W. (1995). The thermosome of Thermoplasma acidophilum and its relationship to the eukaryotic chaperonin TRiC. Eur. J. Biochem. 227, 848-856.
38. Willison, K., and Horwich, A.L. (1996). In: The Chaperonins, R.J. Ellis, ed., (San Diego, CA, USA: Academic Press).
39. Yan, Z., Fujiwara, S., Kohda, K., Takagi, M., and Imanaka, T. (1997). In vitro stabilization and in vivo solubilization of foreign proteins by the β subunit of a chaperonin from the hyperthermophilicarchaeon Pyrococcus sp. strain KOD1. Appl. Environ. Microbiol. 63, 785-789.
40. Yoshida, T., Yohda, M., Iida, T., Maruyama, T., Taguchi, H., Yazaki, K., Ohta, T., Odaka, M., Endo, I., and Kagawa, Y. (1997). Structural and functional characterization of homooligomeric complexes of α and β chaperonin subunits from the hyperthermophilic archaeum Thermococcus strain KS-1. J. Mol. Biol. 273, 635-645.
41. Zettlmeissl, G., Rudolph, R., and Jaenicke, R. (1979). Reconstitution of lactic dehydrogenase. Noncovalent aggregation vs. reactivation. 1. Physical properties and kinetics of aggregation. Biochemistry 18, 5567-5571.