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Volumn 378, Issue 7, 1997, Pages 679-685

The PGK-TIM fusion protein from Thermotoga maritima and its constituent parts are intrinsically stable and fold independently

Author keywords

Glycolysis; PGK; Thermostability; Thermotoga maritima; TIM

Indexed keywords

BACTERIAL ENZYME; GLYCOLYTIC ENZYME; GUANIDINE; HYBRID PROTEIN; PHOSPHOGLYCERATE KINASE; TRIOSEPHOSPHATE ISOMERASE;

EID: 0030810898     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/bchm.1997.378.7.679     Document Type: Article
Times cited : (13)

References (38)
  • 1
    • 0031006209 scopus 로고    scopus 로고
    • Crystallographic analysis of phosphoglycerate kinase from the hyperthermophilic bacterium Thermotoga maritima
    • Auerbach, G., Jacob, U., Grättinger, M., Schurig, H., and Jaenicke, R. (1997). Crystallographic analysis of phosphoglycerate kinase from the hyperthermophilic bacterium Thermotoga maritima. Biol. Chem. 378, 327-329.
    • (1997) Biol. Chem. , vol.378 , pp. 327-329
    • Auerbach, G.1    Jacob, U.2    Grättinger, M.3    Schurig, H.4    Jaenicke, R.5
  • 4
    • 1842289252 scopus 로고
    • Cloning, sequencing, expression and characterization of the gene encoding the PGK-TIM fusion protein from Thermotoga maritima
    • Beaucamp, N., Ostendorp, R., Schurig, H., and Jaenicke, R. (1995). Cloning, sequencing, expression and characterization of the gene encoding the PGK-TIM fusion protein from Thermotoga maritima. Prot. Pept. Lett. 2, 287-290.
    • (1995) Prot. Pept. Lett. , vol.2 , pp. 287-290
    • Beaucamp, N.1    Ostendorp, R.2    Schurig, H.3    Jaenicke, R.4
  • 5
    • 0031030767 scopus 로고    scopus 로고
    • Synergistic effects of substrate-induced conformational changes in PGK activation
    • Bernstein, B.E., Michels, P.A.M., and Hol, W.G.J. (1997). Synergistic effects of substrate-induced conformational changes in PGK activation. Nature 385, 275-278.
    • (1997) Nature , vol.385 , pp. 275-278
    • Bernstein, B.E.1    Michels, P.A.M.2    Hol, W.G.J.3
  • 7
    • 0028085225 scopus 로고
    • Characterization of an ancestral type of pyruvate ferredoxin oxidoreductase from the hyperthermophilic bacterium Thermotoga maritima
    • Blarney, J.M., and Adams, M.W.W. (1994). Characterization of an ancestral type of pyruvate ferredoxin oxidoreductase from the hyperthermophilic bacterium Thermotoga maritima. Biochemistry 33, 585-601.
    • (1994) Biochemistry , vol.33 , pp. 585-601
    • Blarney, J.M.1    Adams, M.W.W.2
  • 8
    • 0001590330 scopus 로고
    • The TIM barrel: The most frequently occuring folding motif in proteins
    • Brändén, C.I. (1991). The TIM barrel: The most frequently occuring folding motif in proteins. Curr. Opin. Struct. Biol. 1, 978-983.
    • (1991) Curr. Opin. Struct. Biol. , vol.1 , pp. 978-983
    • Brändén, C.I.1
  • 9
    • 0015303671 scopus 로고
    • Studies on protein sub-units: II. Preparation and properties of active subunits of aldolase bound to a matrix
    • Chan, W.W.-C., and Mawer, M. (1972). Studies on protein sub-units: II. Preparation and properties of active subunits of aldolase bound to a matrix. Arch. Biochem. Biophys. 149, 136-145.
    • (1972) Arch. Biochem. Biophys. , vol.149 , pp. 136-145
    • Chan, W.W.-C.1    Mawer, M.2
  • 10
    • 0015522150 scopus 로고
    • Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion
    • Chen, Y.H., Yang, J.T., and Martinez, H.M. (1972). Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion. Biochemistry 11, 4120-4131.
    • (1972) Biochemistry , vol.11 , pp. 4120-4131
    • Chen, Y.H.1    Yang, J.T.2    Martinez, H.M.3
  • 12
    • 0028846686 scopus 로고
    • Crystal structure of recombinant triosephosphate isomerase from Bacillus stearothermophilus. An analysis of potential thermostability factors in six isomerases with known three-dimensional structures points to the importance of hydrophobic interactions
    • Delboni, L.F., Mande, S.C., Rentier-Delrue, F., Manfroid, V., Turley, S., Vellieux, F.M.D., Martial, J.A., and Hol, W.G.J. (1995). Crystal structure of recombinant triosephosphate isomerase from Bacillus stearothermophilus. An analysis of potential thermostability factors in six isomerases with known three-dimensional structures points to the importance of hydrophobic interactions. Protein Sci. 4, 2594-2604.
    • (1995) Protein Sci. , vol.4 , pp. 2594-2604
    • Delboni, L.F.1    Mande, S.C.2    Rentier-Delrue, F.3    Manfroid, V.4    Turley, S.5    Vellieux, F.M.D.6    Martial, J.A.7    Hol, W.G.J.8
  • 13
    • 0025284257 scopus 로고
    • The revolution of α/β barrel enzymes
    • Farber, G.K., and Petsko, G.A. (1990). The revolution of α/β barrel enzymes. TIBS 15, 228-234.
    • (1990) TIBS , vol.15 , pp. 228-234
    • Farber, G.K.1    Petsko, G.A.2
  • 14
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill, S.C., and von Hippel, P.H. (1989). Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182, 319-326.
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 15
    • 0022522022 scopus 로고
    • Thermotoga maritima sp. nov. represents a new genus of unique extremely thermophilic eubacteriagrowing up to 90°C
    • Huber, R., Langworthy, T.A., König, H., Thomm, M., Woese, C.R., Sleytr, U.B., and Stetter, K.O. (1986). Thermotoga maritima sp. nov. represents a new genus of unique extremely thermophilic eubacteriagrowing up to 90°C. Arch. Microbiol. 144, 324-333.
    • (1986) Arch. Microbiol. , vol.144 , pp. 324-333
    • Huber, R.1    Langworthy, T.A.2    König, H.3    Thomm, M.4    Woese, C.R.5    Sleytr, U.B.6    Stetter, K.O.7
  • 17
    • 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
  • 18
    • 0030067190 scopus 로고    scopus 로고
    • Stability and folding of ultrastable proteins: Eye lens crystallins and enzymes from thermophiles
    • Jaenicke, R. (1996a). Stability and folding of ultrastable proteins: Eye lens crystallins and enzymes from thermophiles. FASEB J., 10, 84-92.
    • (1996) FASEB J. , vol.10 , pp. 84-92
    • Jaenicke, R.1
  • 19
    • 0029685460 scopus 로고    scopus 로고
    • Protein folding and association: Significance of in vitro studies for self-organization and targeting in the cell
    • Jaenicke, R. (1996b). Protein folding and association: Significance of in vitro studies for self-organization and targeting in the cell. Curr. Top. Cell. Reg. 34, 209-314.
    • (1996) Curr. Top. Cell. Reg. , vol.34 , pp. 209-314
    • Jaenicke, R.1
  • 20
    • 0029786277 scopus 로고    scopus 로고
    • Structure and stability of hyperstable proteins: Glycolytic enzymes from hyperthermophilic bacterium Thermotoga maritima
    • Jaenicke, R., Schurig, H., Beaucamp, N., and Ostendorp, R. (1996). Structure and stability of hyperstable proteins: Glycolytic enzymes from hyperthermophilic bacterium Thermotoga maritima. Adv. Prot. Chem. 48, 181-269.
    • (1996) Adv. Prot. Chem. , vol.48 , pp. 181-269
    • Jaenicke, R.1    Schurig, H.2    Beaucamp, N.3    Ostendorp, R.4
  • 21
    • 0027177819 scopus 로고
    • The anatomy of a kinase and the control of phosphate transfer
    • Joao, H.C., and Williams, R.J.P. (1993). The anatomy of a kinase and the control of phosphate transfer. Eur. J. Biochem. 216, 1-18.
    • (1993) Eur. J. Biochem. , vol.216 , pp. 1-18
    • Joao, H.C.1    Williams, R.J.P.2
  • 22
    • 0028895142 scopus 로고
    • The phosphoglycerate kinase and glyceraldehyde-3-phosphate dehydrogenase genes from the thermophilic archaeon Sulfolobussolfataricus overlap by 8-bp
    • Jones, C.E., Fleming, T.M., Cowan, D.A., Littlechild, J.A., and Piper, P.W. (1995). The phosphoglycerate kinase and glyceraldehyde-3-phosphate dehydrogenase genes from the thermophilic archaeon Sulfolobussolfataricus overlap by 8-bp. Eur. J. Biochem. 233, 800-808.
    • (1995) Eur. J. Biochem. , vol.233 , pp. 800-808
    • Jones, C.E.1    Fleming, T.M.2    Cowan, D.A.3    Littlechild, J.A.4    Piper, P.W.5
  • 23
    • 0025763437 scopus 로고
    • Enzyme catalysis: Not different, just better
    • Knowles, J.R. (1991). Enzyme catalysis: not different, just better. Nature 350, 121-124.
    • (1991) Nature , vol.350 , pp. 121-124
    • Knowles, J.R.1
  • 24
    • 0028296717 scopus 로고
    • Triosephosphate isomerase requires a positively charged active site: The role of lysine-12
    • Lodi, P.J., Chang, L.C., Knowles, J.R., and Komives, E.A. (1994). Triosephosphate isomerase requires a positively charged active site: The role of lysine-12. Biochemistry 33, 2809-2814.
    • (1994) Biochemistry , vol.33 , pp. 2809-2814
    • Lodi, P.J.1    Chang, L.C.2    Knowles, J.R.3    Komives, E.A.4
  • 26
    • 0023020019 scopus 로고
    • Evolutionary conservation of the substrate-binding cleft of phosphoglycerate kinases
    • Mori, N., Singer-Sam, J., and Riggs, A.D. (1986). Evolutionary conservation of the substrate-binding cleft of phosphoglycerate kinases. FEBS Lett. 204, 313-317.
    • (1986) FEBS Lett. , vol.204 , pp. 313-317
    • Mori, N.1    Singer-Sam, J.2    Riggs, A.D.3
  • 27
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace, C.N., Vajdos, F., Fee, L., Grimsley, G., and Grey, T. (1995). How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 4, 2411-2423.
    • (1995) Protein Sci. , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Grey, T.5
  • 28
    • 0028356024 scopus 로고
    • 2 in the anaerobic hyperthermophilic eubacterium Thermotoga maritima: Involvement of the Embden-Meyerhof pathway
    • 2 in the anaerobic hyperthermophilic eubacterium Thermotoga maritima: Involvement of the Embden-Meyerhof pathway. Arch. Microbiol. 161, 460-470.
    • (1994) Arch. Microbiol. , vol.161 , pp. 460-470
    • Schröder, C.1    Selig, M.2    Schönheit, P.3
  • 29
    • 0026648514 scopus 로고
    • Stability and reconstitution of D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic eubacterium Thermotoga maritima
    • Rehaber, V., and Jaenicke, R. (1992). Stability and reconstitution of D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic eubacterium Thermotoga maritima. J. Biol. Chem. 267, 10999-11006.
    • (1992) J. Biol. Chem. , vol.267 , pp. 10999-11006
    • Rehaber, V.1    Jaenicke, R.2
  • 32
    • 0028819196 scopus 로고
    • Phosphoglycerate kinase and triose-phosphate isomerase from the hyperthermophilic bacterium Thermotoga maritima form a covalent bifunctional enzyme complex
    • Schurig, H., Beaucamp, N., Ostendorp, R., Jaenicke, R., Adler, E., and Knowles, J.R. (1995). Phosphoglycerate kinase and triose-phosphate isomerase from the hyperthermophilic bacterium Thermotoga maritima form a covalent bifunctional enzyme complex. EMBO J. 14, 442-451.
    • (1995) EMBO J. , vol.14 , pp. 442-451
    • Schurig, H.1    Beaucamp, N.2    Ostendorp, R.3    Jaenicke, R.4    Adler, E.5    Knowles, J.R.6
  • 33
    • 0025238762 scopus 로고
    • Isoenzymes of phosphoglycerate kinase: Evolutionary conservation of structure of this glycolytic enzyme
    • Watson, H.C., and Littlechild, J.A. (1990). Isoenzymes of phosphoglycerate kinase: Evolutionary conservation of structure of this glycolytic enzyme. Biochem. Soc. Trans. 18, 187-190.
    • (1990) Biochem. Soc. Trans. , vol.18 , pp. 187-190
    • Watson, H.C.1    Littlechild, J.A.2
  • 34
    • 0026519169 scopus 로고
    • Comparison of the refined crystal structures of liganded and unliganded chicken, yeast and trypanosomal triosephosphate isomerase
    • Wierenga, R.K., Noble, M.E.M., and Davenport, R.C. (1992). Comparison of the refined crystal structures of liganded and unliganded chicken, yeast and trypanosomal triosephosphate isomerase. J. Mol. Biol. 224, 1115-1126.
    • (1992) J. Mol. Biol. , vol.224 , pp. 1115-1126
    • Wierenga, R.K.1    Noble, M.E.M.2    Davenport, R.C.3
  • 35
    • 0013483235 scopus 로고
    • GAPDH from the extreme thermophilic eubacterium Thermotoga maritima
    • Wrba, A., Schweiger, A., Schultes, V., Jaenicke, R., and Závodszky, P. (1990). GAPDH from the extreme thermophilic eubacterium Thermotoga maritima. Biochemistry 29, 7585-7592.
    • (1990) Biochemistry , vol.29 , pp. 7585-7592
    • Wrba, A.1    Schweiger, A.2    Schultes, V.3    Jaenicke, R.4    Závodszky, P.5
  • 37
    • 0019089331 scopus 로고
    • Folding and association of TIM from rabbit muscle
    • Zabori, S., Rudolph, R., and Jaenicke, R. (1980). Folding and association of TIM from rabbit muscle. Z. Naturforsch. 35c, 999-1004.
    • (1980) Z. Naturforsch. , vol.35 C , pp. 999-1004
    • Zabori, S.1    Rudolph, R.2    Jaenicke, R.3
  • 38
    • 0018788361 scopus 로고
    • Reconstitution of lactate dehydrogenase: Non-covalent aggregation versus reactivation. I. Physical properties and kinetics of aggregation
    • Zettlmeissl, G., Rudolph, R., and Jaenicke, R. (1979). Reconstitution of lactate dehydrogenase: non-covalent aggregation versus reactivation. I. Physical properties and kinetics of aggregation. Biochemistry 18, 5567-5571.
    • (1979) Biochemistry , vol.18 , pp. 5567-5571
    • Zettlmeissl, G.1    Rudolph, R.2    Jaenicke, R.3


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