메뉴 건너뛰기




Volumn 54, Issue 4, 1998, Pages 372-377

β-lactamases as models for protein-folding studies

Author keywords

lactamase; cis trans isomerization; Folding intermediates; Molten globule; Protein folding

Indexed keywords

ACRYLAMIDE; BETA LACTAMASE; PROLINE; TRYPTOPHAN;

EID: 0031923940     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s000180050166     Document Type: Conference Paper
Times cited : (23)

References (36)
  • 1
    • 0016839297 scopus 로고
    • The amino acid sequence of Staphylococcus aureus penicillinase
    • Ambler R. P. (1975) The amino acid sequence of Staphylococcus aureus penicillinase. Biochem. J. 151: 197-218
    • (1975) Biochem. J. , vol.151 , pp. 197-218
    • Ambler, R.P.1
  • 2
    • 0000721718 scopus 로고
    • Analysis by transduction of mutations affecting penicillinase formation in Staphylococcus aureus
    • Novick R. P. (1963) Analysis by transduction of mutations affecting penicillinase formation in Staphylococcus aureus. J. Gen. Microbiol. 33: 121-136
    • (1963) J. Gen. Microbiol. , vol.33 , pp. 121-136
    • Novick, R.P.1
  • 3
    • 0023204095 scopus 로고
    • Bacterial resistance to β-lactam antibiotics: Crystal structure of β-lactamase from Staphylococcus aureus PC1 at 2.5 Å resolution
    • Herzberg O. and Moult J. (1987) Bacterial resistance to β-lactam antibiotics: crystal structure of β-lactamase from Staphylococcus aureus PC1 at 2.5 Å resolution. Science 236: 694-701
    • (1987) Science , vol.236 , pp. 694-701
    • Herzberg, O.1    Moult, J.2
  • 4
    • 0026016867 scopus 로고
    • Refined crystal structure of β-lactamase from Staphylococcus aureus PC1 at 2.0 Å resolution
    • Herzberg O. (1991) Refined crystal structure of β-lactamase from Staphylococcus aureus PC1 at 2.0 Å resolution. J. Mol. Biol. 217: 701-719
    • (1991) J. Mol. Biol. , vol.217 , pp. 701-719
    • Herzberg, O.1
  • 5
    • 0020024242 scopus 로고
    • Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding
    • Kim P. S. and Baldwin R. L. (1982) Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding. Annu. Rev. Biochem. 51: 459-489
    • (1982) Annu. Rev. Biochem. , vol.51 , pp. 459-489
    • Kim, P.S.1    Baldwin, R.L.2
  • 7
    • 0017111896 scopus 로고
    • The mechanism of folding of globular proteins. Equilibria and kinetics of conformational transitions of penicillinase from Staphylococcus aureus involving a state of intermediate conformation
    • Robson B. and Pain R. H. (1976) The mechanism of folding of globular proteins. Equilibria and kinetics of conformational transitions of penicillinase from Staphylococcus aureus involving a state of intermediate conformation. Biochem. J. 155: 331-344
    • (1976) Biochem. J. , vol.155 , pp. 331-344
    • Robson, B.1    Pain, R.H.2
  • 8
    • 0002940127 scopus 로고
    • The Molten Globule State
    • Creighton T. E. (ed.). W. H. Freeman, New York
    • Ptitsyn O. B. (1992) The Molten Globule State. In: Protein Folding, pp. 243-300, Creighton T. E. (ed.). W. H. Freeman, New York
    • (1992) Protein Folding , pp. 243-300
    • Ptitsyn, O.B.1
  • 9
    • 3743125499 scopus 로고
    • The role of folding units in the kinetic folding of globular proteins
    • Jaenicke R. (ed.), Elsevier, Amsterdam
    • Adams B., Burgess R. J., Carrey E. A., Mackintosh I. R., Mitchinson C., Thomas R. M. et al. (1980) The role of folding units in the kinetic folding of globular proteins. In: Protein Folding, pp. 447-467, Jaenicke R. (ed.), Elsevier, Amsterdam
    • (1980) Protein Folding , pp. 447-467
    • Adams, B.1    Burgess, R.J.2    Carrey, E.A.3    Mackintosh, I.R.4    Mitchinson, C.5    Thomas, R.M.6
  • 10
    • 0021885917 scopus 로고
    • Effects of sulphate and urea on the stability and reversible unfolding of β-lactamase from Staphylococcus aureus: Implications for the folding pathway of β-lactamase
    • Mitchinson C. and Pain R. H. (1985) Effects of sulphate and urea on the stability and reversible unfolding of β-lactamase from Staphylococcus aureus: implications for the folding pathway of β-lactamase. J. Mol. Biol. 184: 331-342
    • (1985) J. Mol. Biol. , vol.184 , pp. 331-342
    • Mitchinson, C.1    Pain, R.H.2
  • 11
    • 0029888845 scopus 로고    scopus 로고
    • The rate limiting step in the folding of the cis-Pro167Thr mutant of TEM-1 β-lactamase is the trans to cis isomerization of a non-proline peptide bond
    • Vanhove M., Raquet X., Palzkill T., Pain R. H. and Frère J.-M. (1996) The rate limiting step in the folding of the cis-Pro167Thr mutant of TEM-1 β-lactamase is the trans to cis isomerization of a non-proline peptide bond. Proteins 25: 104-111
    • (1996) Proteins , vol.25 , pp. 104-111
    • Vanhove, M.1    Raquet, X.2    Palzkill, T.3    Pain, R.H.4    Frère, J.-M.5
  • 12
    • 0024963570 scopus 로고
    • Conformational states of β-lactamase: Molten globule states at acid and alkaline pH with high salt
    • Goto Y. and Fink A. L. (1989) Conformational states of β-lactamase: molten globule states at acid and alkaline pH with high salt. Biochemistry 28: 945-952
    • (1989) Biochemistry , vol.28 , pp. 945-952
    • Goto, Y.1    Fink, A.L.2
  • 13
    • 0025212107 scopus 로고
    • Evidence for a molten globule state as a general intermediate in protein folding
    • Ptitsyn O. B., Pain R. H., Semisotnov G. V., Žerovnik E. and Razgulyaev O. I. (1990) Evidence for a molten globule state as a general intermediate in protein folding. FEBS Lett. 262: 20-24
    • (1990) FEBS Lett. , vol.262 , pp. 20-24
    • Ptitsyn, O.B.1    Pain, R.H.2    Semisotnov, G.V.3    Žerovnik, E.4    Razgulyaev, O.I.5
  • 14
    • 0019324857 scopus 로고
    • Unfolding and refolding of Staphylococcus aureus penicillinase by urea-gradient electrophoresis
    • Creighton T. E. and Pain R. H. (1980) Unfolding and refolding of Staphylococcus aureus penicillinase by urea-gradient electrophoresis. J. Mol. Biol. 137: 431-436
    • (1980) J. Mol. Biol. , vol.137 , pp. 431-436
    • Creighton, T.E.1    Pain, R.H.2
  • 15
    • 0023041667 scopus 로고
    • Evidence for identity between the equilibrium folded intermediate and a transient folding intermediate: A comparative study of the folding reactions of α-lactalbumin and lysozyme
    • Ikeguchi M., Kuwajima K., Mitani M. and Sugai S. (1986) Evidence for identity between the equilibrium folded intermediate and a transient folding intermediate: a comparative study of the folding reactions of α-lactalbumin and lysozyme. Biochemistry 25: 6965-6972
    • (1986) Biochemistry , vol.25 , pp. 6965-6972
    • Ikeguchi, M.1    Kuwajima, K.2    Mitani, M.3    Sugai, S.4
  • 16
    • 0031837168 scopus 로고    scopus 로고
    • Protein folding: Matching theory and experiment
    • in press
    • Laurents D. V. and Baldwin R. E. (1998) Protein folding: matching theory and experiment. Biophys. J., in press
    • (1998) Biophys. J.
    • Laurents, D.V.1    Baldwin, R.E.2
  • 17
    • 0027432676 scopus 로고
    • Secondary structure of globular proteins at the early and final stages in protein folding
    • Kuwajima K., Semisotnov G. V., Finkelstein A. V., Sugai S. and Ptitsyn O. B. (1993) Secondary structure of globular proteins at the early and final stages in protein folding. FEBS Lett. 334: 265-268
    • (1993) FEBS Lett. , vol.334 , pp. 265-268
    • Kuwajima, K.1    Semisotnov, G.V.2    Finkelstein, A.V.3    Sugai, S.4    Ptitsyn, O.B.5
  • 18
    • 0032539580 scopus 로고    scopus 로고
    • A collapsed intermediate with non-native packing of hydrophobic residues in the folding of TEM-1 β-lactamase
    • Vanhove M., Lejeune A., Guillaume G., Virden R., Pain R. H., Schmid F. X. et al. (1998) A collapsed intermediate with non-native packing of hydrophobic residues in the folding of TEM-1 β-lactamase. Biochemistry 37: 1941-1950
    • (1998) Biochemistry , vol.37 , pp. 1941-1950
    • Vanhove, M.1    Lejeune, A.2    Guillaume, G.3    Virden, R.4    Pain, R.H.5    Schmid, F.X.6
  • 19
    • 0343852923 scopus 로고    scopus 로고
    • Folding intermediates of β-lactamase recognized by GroEL
    • Gervasoni P. and Plückthun A. (1997) Folding intermediates of β-lactamase recognized by GroEL. FEBS Lett. 401: 138-142
    • (1997) FEBS Lett. , vol.401 , pp. 138-142
    • Gervasoni, P.1    Plückthun, A.2
  • 20
    • 0029740071 scopus 로고    scopus 로고
    • Non-native α-helical intermediate in the refolding of β-lactoglobulin, a predominantly β-sheet protein
    • Hamada D., Segawa S. and Goto Y. (1996) Non-native α-helical intermediate in the refolding of β-lactoglobulin, a predominantly β-sheet protein. Nature Struct. Biol. 3: 868-873
    • (1996) Nature Struct. Biol. , vol.3 , pp. 868-873
    • Hamada, D.1    Segawa, S.2    Goto, Y.3
  • 21
    • 0026751786 scopus 로고
    • The folding of hen lysozyme involves partially structured intermediates and multiple pathways
    • Radford S. E., Dobson C. M. and Evans P. A. (1992) The folding of hen lysozyme involves partially structured intermediates and multiple pathways. Nature 358: 302-307
    • (1992) Nature , vol.358 , pp. 302-307
    • Radford, S.E.1    Dobson, C.M.2    Evans, P.A.3
  • 22
    • 0028227296 scopus 로고
    • Tertiary interactions in the folding pathway of hen lysozyme: Kinetic studies using fluorescent probes
    • Itzhaki L. S., Evans P. A., Dobson C. M. and Radford S. E. (1994) Tertiary interactions in the folding pathway of hen lysozyme: kinetic studies using fluorescent probes. Biochemistry 33: 5212-5220
    • (1994) Biochemistry , vol.33 , pp. 5212-5220
    • Itzhaki, L.S.1    Evans, P.A.2    Dobson, C.M.3    Radford, S.E.4
  • 23
    • 0027936262 scopus 로고
    • Kinetics of folding of guanidine-denatured hen egg white lysozyme and carboxymethyl(Cys6,Cys127)-lysozyme: A stopped-flow absorbance and fluorescence study
    • Denton M. E., Rothwarf D. M. and Scheraga H. A. (1994) Kinetics of folding of guanidine-denatured hen egg white lysozyme and carboxymethyl(Cys6,Cys127)-lysozyme: a stopped-flow absorbance and fluorescence study. Biochemistry 33: 11225-11236
    • (1994) Biochemistry , vol.33 , pp. 11225-11236
    • Denton, M.E.1    Rothwarf, D.M.2    Scheraga, H.A.3
  • 24
    • 0029904097 scopus 로고    scopus 로고
    • Role of non-native aromatic and hydrophobic interactions in the folding of hen egg white lysozyme
    • Rothwarf D. M. and Scheraga H. A. (1996) Role of non-native aromatic and hydrophobic interactions in the folding of hen egg white lysozyme. Biochemistry 35: 13797-13807
    • (1996) Biochemistry , vol.35 , pp. 13797-13807
    • Rothwarf, D.M.1    Scheraga, H.A.2
  • 25
    • 0027275788 scopus 로고
    • Crystal structure of Escherichia coli TEM1 β-lactamase at 1.8 Å resolution
    • Jelsch C., Mourey L., Masson J.-M. and Samama J.-P. (1993) Crystal structure of Escherichia coli TEM1 β-lactamase at 1.8 Å resolution. Proteins 16: 364-383
    • (1993) Proteins , vol.16 , pp. 364-383
    • Jelsch, C.1    Mourey, L.2    Masson, J.-M.3    Samama, J.-P.4
  • 26
    • 0026801518 scopus 로고
    • Molecular structure of the acyl-enzyme intermediate in β-lactam hydrolysis at 1.7 Å resolution
    • Strynadka N. C. J., Adachi H., Jensen S. E., Johns K., Sielecki A., Betzel C. et al. (1992) Molecular structure of the acyl-enzyme intermediate in β-lactam hydrolysis at 1.7 Å resolution. Nature 359: 700-705
    • (1992) Nature , vol.359 , pp. 700-705
    • Strynadka, N.C.J.1    Adachi, H.2    Jensen, S.E.3    Johns, K.4    Sielecki, A.5    Betzel, C.6
  • 27
    • 0024363590 scopus 로고
    • The precursor of β-lactamase: Purification, properties and folding kinetics
    • Laminet A. A. and Plückthun A. (1989) The precursor of β-lactamase: purification, properties and folding kinetics. EMBO J. 8: 1469-1477
    • (1989) EMBO J. , vol.8 , pp. 1469-1477
    • Laminet, A.A.1    Plückthun, A.2
  • 28
    • 0023630729 scopus 로고
    • Stability of wild-type and mutant RTEM-1 β-lactamases: Effect of the disulfide bond
    • Schultz S. C., Dalhadie-McFarland G., Neitzel J. J. and Richards J. H. (1987) Stability of wild-type and mutant RTEM-1 β-lactamases: effect of the disulfide bond. Proteins 2: 290-297
    • (1987) Proteins , vol.2 , pp. 290-297
    • Schultz, S.C.1    Dalhadie-McFarland, G.2    Neitzel, J.J.3    Richards, J.H.4
  • 29
    • 0031026028 scopus 로고    scopus 로고
    • Kinetic and thermodynamic consequences of the removal of the Cys-77 Cys-123 disulphide bond for the folding of TEM-1 β-lactamase
    • Vanhove M., Guillaume G., Ledent P., Richards J. H., Pain R. H. and Frère J.-M. (1997) Kinetic and thermodynamic consequences of the removal of the Cys-77 Cys-123 disulphide bond for the folding of TEM-1 β-lactamase. Biochem. J. 321: 413-417
    • (1997) Biochem. J. , vol.321 , pp. 413-417
    • Vanhove, M.1    Guillaume, G.2    Ledent, P.3    Richards, J.H.4    Pain, R.H.5    Frère, J.-M.6
  • 30
    • 0028034273 scopus 로고
    • Effect of redox environment on the in vitro and in vivo folding of RTEM-1 β-lactamase and Escherichia coli alkaline phosphatase
    • Walker K. W. and Gilbert H. F. (1994) Effect of redox environment on the in vitro and in vivo folding of RTEM-1 β-lactamase and Escherichia coli alkaline phosphatase. J. Biol. Chem. 269: 28487-28493
    • (1994) J. Biol. Chem. , vol.269 , pp. 28487-28493
    • Walker, K.W.1    Gilbert, H.F.2
  • 31
    • 0028785706 scopus 로고
    • Oxidation of kinetically trapped thiols by protein disulfide isomerase
    • Walker K. W. and Gilbert H. F. (1995) Oxidation of kinetically trapped thiols by protein disulfide isomerase. Biochemistry 34: 13642-13650
    • (1995) Biochemistry , vol.34 , pp. 13642-13650
    • Walker, K.W.1    Gilbert, H.F.2
  • 32
    • 0029781655 scopus 로고    scopus 로고
    • Competition between DsbA-mediated oxidation and conformational folding of RTEM-1 β-lactamase
    • Frech C., Wunderlich M., Glockshuber R. and Schmid F. X. (1996) Competition between DsbA-mediated oxidation and conformational folding of RTEM-1 β-lactamase. Biochemistry 35: 11386-11395
    • (1996) Biochemistry , vol.35 , pp. 11386-11395
    • Frech, C.1    Wunderlich, M.2    Glockshuber, R.3    Schmid, F.X.4
  • 33
    • 0029063334 scopus 로고
    • Investigation of the folding pathway of the TEM-1 β-lactamase
    • Vanhove M., Raquet X. and Frère J.-M. (1995) Investigation of the folding pathway of the TEM-1 β-lactamase. Proteins 22: 110-118
    • (1995) Proteins , vol.22 , pp. 110-118
    • Vanhove, M.1    Raquet, X.2    Frère, J.-M.3
  • 34
    • 0016711868 scopus 로고
    • Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues
    • Brandts J. F., Halvorson H. R. and Brennan M. (1975) Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues. Biochemistry 14: 4953-4963
    • (1975) Biochemistry , vol.14 , pp. 4953-4963
    • Brandts, J.F.1    Halvorson, H.R.2    Brennan, M.3
  • 35
    • 0025998489 scopus 로고
    • Structural basis for the inactivation of the P54 mutant of β-lactamase from Staphylococcus aureus PC1
    • Herzberg O., Kapadia G., Blanco B., Smith T. S. and Coulson A. (1991) Structural basis for the inactivation of the P54 mutant of β-lactamase from Staphylococcus aureus PC1. Biochemistry 30: 9503-9509
    • (1991) Biochemistry , vol.30 , pp. 9503-9509
    • Herzberg, O.1    Kapadia, G.2    Blanco, B.3    Smith, T.S.4    Coulson, A.5
  • 36
    • 0022394785 scopus 로고
    • Single amino acid mutations block a late step in the folding of β-lactamase from Staphylococcus aureus
    • Craig S., Hollecker M., Creighton T. E. and Pain R. H. (1985) Single amino acid mutations block a late step in the folding of β-lactamase from Staphylococcus aureus. J. Mol. Biol. 185: 681-687
    • (1985) J. Mol. Biol. , vol.185 , pp. 681-687
    • Craig, S.1    Hollecker, M.2    Creighton, T.E.3    Pain, R.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.