메뉴 건너뛰기




Volumn 42, Issue 10, 2003, Pages 3105-3112

Demonstration of two independently folding domains in the α subunit of bacterial luciferase by preferential ligand binding-induced stabilization

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; CHROMATOGRAPHIC ANALYSIS; NEGATIVE IONS; POLYPEPTIDES;

EID: 0037452956     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi026725s     Document Type: Article
Times cited : (5)

References (54)
  • 1
    • 0019489088 scopus 로고
    • Folding of protein fragments
    • Wetlaufer, D. B. (1981) Folding of protein fragments. Adv. Protein Chem. 34, 61-92.
    • (1981) Adv. Protein Chem. , vol.34 , pp. 61-92
    • Wetlaufer, D.B.1
  • 2
    • 0029027663 scopus 로고
    • Three-dimensional structure of bacterial luciferase from Vibrio harveyi at 2.4 Å resolution
    • Fisher, A. J., Raushel, F. M., Baldwin, T. O., and Rayment, I. (1995) Three-dimensional structure of bacterial luciferase from Vibrio harveyi at 2.4 Å resolution. Biochemistry 34, 6581-6586.
    • (1995) Biochemistry , vol.34 , pp. 6581-6586
    • Fisher, A.J.1    Raushel, F.M.2    Baldwin, T.O.3    Rayment, I.4
  • 3
    • 0029664970 scopus 로고    scopus 로고
    • The 1.5-Å resolution crystal structure of bacterial luciferase in low salt conditions
    • Fisher, A. J., Thompson, T. B., Thoden, J. B., Baldwin, T. O., and Rayment, I. (1996) The 1.5-Å resolution crystal structure of bacterial luciferase in low salt conditions. J. Biol. Chem. 271, 21956-21968.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21956-21968
    • Fisher, A.J.1    Thompson, T.B.2    Thoden, J.B.3    Baldwin, T.O.4    Rayment, I.5
  • 4
    • 0027241972 scopus 로고
    • Refolding of luciferase subunits from urea and assembly of the active heterodimer. Evidence for folding intermediates that precede and follow the dimerization step on the pathway to the active form of the enzyme
    • Ziegler, M. M., Goldberg, M. E., Chaffotte, A. F., and Baldwin, T. O. (1993) Refolding of luciferase subunits from urea and assembly of the active heterodimer. Evidence for folding intermediates that precede and follow the dimerization step on the pathway to the active form of the enzyme. J. Biol. Chem. 268, 10760-10765.
    • (1993) J. Biol. Chem. , vol.268 , pp. 10760-10765
    • Ziegler, M.M.1    Goldberg, M.E.2    Chaffotte, A.F.3    Baldwin, T.O.4
  • 5
    • 0027178317 scopus 로고
    • Contribution of folding steps involving the individual subunits of bacterial luciferase to the assembly of the active heterodimeric enzyme
    • Baldwin, T. O., Ziegler, M. M., Chaffotte, A. F., and Goldberg, M. E. (1993) Contribution of folding steps involving the individual subunits of bacterial luciferase to the assembly of the active heterodimeric enzyme. J. Biol. Chem. 268, 10766-10772.
    • (1993) J. Biol. Chem. , vol.268 , pp. 10766-10772
    • Baldwin, T.O.1    Ziegler, M.M.2    Chaffotte, A.F.3    Goldberg, M.E.4
  • 7
    • 0027162959 scopus 로고
    • Folding of bacterial luciferase involves a non-native heterodimeric intermediate in equilibrium with the native enzyme and the unfolded subunits
    • Clark, A. C., Sinclair, J. F., and Baldwin, T. O. (1993) Folding of bacterial luciferase involves a non-native heterodimeric intermediate in equilibrium with the native enzyme and the unfolded subunits. J. Biol. Chem. 268, 10773-10779.
    • (1993) J. Biol. Chem. , vol.268 , pp. 10773-10779
    • Clark, A.C.1    Sinclair, J.F.2    Baldwin, T.O.3
  • 8
    • 0028426938 scopus 로고
    • Kinetic partitioning during protein folding yields multiple native states
    • Sinclair, J. F., Ziegler, M. M., and Baldwin, T. O. (1994) Kinetic partitioning during protein folding yields multiple native states. Nat. Struct. Biol. 1, 320-326.
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 320-326
    • Sinclair, J.F.1    Ziegler, M.M.2    Baldwin, T.O.3
  • 9
    • 0027241920 scopus 로고
    • Purified native subunits of bacterial luciferase are active in the bioluminescence reaction but fail to assemble into the alpha beta structure
    • Sinclair, J. F., Waddle, J. J., Waddill, E. F., and Baldwin, T. O. (1993) Purified native subunits of bacterial luciferase are active in the bioluminescence reaction but fail to assemble into the alpha beta structure. Biochemistry 32, 5036-5044.
    • (1993) Biochemistry , vol.32 , pp. 5036-5044
    • Sinclair, J.F.1    Waddle, J.J.2    Waddill, E.F.3    Baldwin, T.O.4
  • 12
    • 0033534148 scopus 로고    scopus 로고
    • Folding, stability, and physical properties of the alpha subunit of bacterial luciferase
    • Noland, B. W., Dangott, L. J., and Baldwin, T. O. (1999) Folding, stability, and physical properties of the alpha subunit of bacterial luciferase. Biochemistry 38, 16136-16145.
    • (1999) Biochemistry , vol.38 , pp. 16136-16145
    • Noland, B.W.1    Dangott, L.J.2    Baldwin, T.O.3
  • 14
    • 0015919524 scopus 로고
    • Flavine specificity of enzyme-substrate intermediates in the bacterial bioluminescent reaction. Structural requirements of the flavine side chain
    • Meighen, E. A., and MacKenzie, R. E. (1973) Flavine specificity of enzyme-substrate intermediates in the bacterial bioluminescent reaction. Structural requirements of the flavine side chain. Biochemistry 12, 1482-1491.
    • (1973) Biochemistry , vol.12 , pp. 1482-1491
    • Meighen, E.A.1    MacKenzie, R.E.2
  • 15
    • 0346000058 scopus 로고
    • Anion binding to bacterial luciferase: Evidence for binding associated changes in enzyme structure
    • Yagi, K., and Yamano, T., Eds., University Park Press, Baltimore, MD
    • Baldwin, T. O., and Riley, P. L. (1980) Anion binding to bacterial luciferase: evidence for binding associated changes in enzyme structure, in Flavins and Flavoproteins (Yagi, K., and Yamano, T., Eds.) pp 139-147, University Park Press, Baltimore, MD.
    • (1980) Flavins and Flavoproteins , pp. 139-147
    • Baldwin, T.O.1    Riley, P.L.2
  • 16
    • 0019085525 scopus 로고
    • Proteolytic inactivation of luciferases from three species of luminous marine bacteria, Beneckea harveyi, Photobacterium fischeri, and Photobacterium phosphoreum: Evidence of a conserved structural feature
    • Holzman, T. F., and Baldwin, T. O. (1980) Proteolytic inactivation of luciferases from three species of luminous marine bacteria, Beneckea harveyi, Photobacterium fischeri, and Photobacterium phosphoreum: evidence of a conserved structural feature. Proc. Natl. Acad. Sci. U.S.A. 77, 6363-6367.
    • (1980) Proc. Natl. Acad. Sci. U.S.A. , vol.77 , pp. 6363-6367
    • Holzman, T.F.1    Baldwin, T.O.2
  • 17
    • 0021860683 scopus 로고
    • Nucleotide sequence of the luxA gene of Vibrio harveyi and the complete amino acid sequence of the α subunit of bacterial luciferase
    • Cohn, D. H., Mileham, A. J., Simon, M. I., Nealson, K. H., Rausch, S. K., Bonam, D., and Baldwin, T. O. (1985) Nucleotide sequence of the luxA gene of Vibrio harveyi and the complete amino acid sequence of the α subunit of bacterial luciferase. J. Biol. Chem. 260, 6139-6146.
    • (1985) J. Biol. Chem. , vol.260 , pp. 6139-6146
    • Cohn, D.H.1    Mileham, A.J.2    Simon, M.I.3    Nealson, K.H.4    Rausch, S.K.5    Bonam, D.6    Baldwin, T.O.7
  • 18
    • 84915870695 scopus 로고
    • Structural analysis of fragments resulting from limited proteolysis of bacterial luciferase
    • Massey, V., and Williams, C. H., Eds., Elsevier North-Holland, Inc., New York
    • Rausch, S. K., Dougherty, J. I., Jr., and Baldwin, T. O. (1982) Structural analysis of fragments resulting from limited proteolysis of bacterial luciferase, in Flavins and Flavoproteins (Massey, V., and Williams, C. H., Eds.) pp 375-378, Elsevier North-Holland, Inc., New York.
    • (1982) Flavins and Flavoproteins , pp. 375-378
    • Rausch, S.K.1    Dougherty J.I., Jr.2    Baldwin, T.O.3
  • 19
    • 0033931440 scopus 로고    scopus 로고
    • Overexpression of bacterial luciferase and purification from recombinant sources
    • Baldwin, T. O., Ziegler, M. M., Green, V. A., and Thomas, M. D. (2000) Overexpression of bacterial luciferase and purification from recombinant sources. Methods Enzymol. 305, 135-152.
    • (2000) Methods Enzymol. , vol.305 , pp. 135-152
    • Baldwin, T.O.1    Ziegler, M.M.2    Green, V.A.3    Thomas, M.D.4
  • 20
    • 0033935798 scopus 로고    scopus 로고
    • Overexpression of foreign proteins using the Vibrio fischeri lux control system
    • Thomas, M. D., and van Tilburg, A. (2000) Overexpression of foreign proteins using the Vibrio fischeri lux control system. Methods Enzymol. 305, 315-329.
    • (2000) Methods Enzymol. , vol.305 , pp. 315-329
    • Thomas, M.D.1    Van Tilburg, A.2
  • 21
    • 0027378450 scopus 로고
    • Resolution of the fluorescence equilibrium unfolding profile of trp aporepressor using single tryptophan mutants
    • Royer, C. A., Mann, C. J., and Matthews, C. R. (1993) Resolution of the fluorescence equilibrium unfolding profile of trp aporepressor using single tryptophan mutants. Protein Sci. 2, 1844-1852.
    • (1993) Protein Sci. , vol.2 , pp. 1844-1852
    • Royer, C.A.1    Mann, C.J.2    Matthews, C.R.3
  • 22
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants
    • Santoro, M. M., and Bolen, D. W. (1988) Unfolding free energy changes determined by the linear extrapolation method. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants. Biochemistry 27, 8063-8068.
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 25
    • 0000802647 scopus 로고
    • The biochemistry and molecular biology of bacterial bioluminescence
    • Müller, F., Ed., CRC Press, Boca Raton, FL
    • Baldwin, T. O., and Ziegler, M. M. (1992) The biochemistry and molecular biology of bacterial bioluminescence, in Chemistry and Biochemistry of Flavoproteins (Müller, F., Ed.) pp 467-530, CRC Press, Boca Raton, FL.
    • (1992) Chemistry and Biochemistry of Flavoproteins , pp. 467-530
    • Baldwin, T.O.1    Ziegler, M.M.2
  • 27
    • 0034918673 scopus 로고    scopus 로고
    • Modeling of the bacterial luciferase-flavin mononucleotide complex combining flexible docking with structure - Activity data
    • Lin, L. Y.-C., Sulea, T., Szittner, R., Vassilyev, V., Purisima, E. O., and Meighen, E. A. (2001) Modeling of the bacterial luciferase-flavin mononucleotide complex combining flexible docking with structure - activity data. Protein Sci. 10, 1563-1571.
    • (2001) Protein Sci. , vol.10 , pp. 1563-1571
    • Lin, L.Y.-C.1    Sulea, T.2    Szittner, R.3    Vassilyev, V.4    Purisima, E.O.5    Meighen, E.A.6
  • 29
    • 0028845170 scopus 로고
    • Tryptophan 250 on the alpha subunit plays an important role in flavin and aldehyde binding to bacterial luciferase. Effects of W → Y mutations on catalytic function
    • Li, Z., and Meighen, E. A. (1995) Tryptophan 250 on the alpha subunit plays an important role in flavin and aldehyde binding to bacterial luciferase. Effects of W → Y mutations on catalytic function. Biochemistry 34, 15084-15090.
    • (1995) Biochemistry , vol.34 , pp. 15084-15090
    • Li, Z.1    Meighen, E.A.2
  • 30
    • 0033214557 scopus 로고    scopus 로고
    • Relationship between the conserved alpha subunit arginine 107 and effects of phosphate on the activity and stability of Vibrio harveyi luciferase
    • Moore, C., Lei, B., and Tu, S.-C. (1999) Relationship between the conserved alpha subunit arginine 107 and effects of phosphate on the activity and stability of Vibrio harveyi luciferase. Arch. Biochem. Biophys. 370, 45-50.
    • (1999) Arch. Biochem. Biophys. , vol.370 , pp. 45-50
    • Moore, C.1    Lei, B.2    Tu, S.-C.3
  • 31
    • 0020490638 scopus 로고
    • Guanidine hydrochloride induced unfolding of the α subunit of tryptophan synthase and two proteolytic fragments: Evidence for stepwise unfolding of the two domains
    • Miles, E. W., Yutani, K., and Ogasahara, K. (1982) Guanidine hydrochloride induced unfolding of the α subunit of tryptophan synthase and two proteolytic fragments: Evidence for stepwise unfolding of the two domains. Biochemistry 21, 2586-2592.
    • (1982) Biochemistry , vol.21 , pp. 2586-2592
    • Miles, E.W.1    Yutani, K.2    Ogasahara, K.3
  • 32
    • 0026685018 scopus 로고
    • Stable substructures of 8-fold αβ-barrel proteins: Fragment complementation of phosphoribosylanthranilate isomerase
    • Elder, J., and Kirschner, K. (1992) Stable substructures of 8-fold αβ-barrel proteins: Fragment complementation of phosphoribosylanthranilate isomerase. Biochemistry 31, 3617-3625.
    • (1992) Biochemistry , vol.31 , pp. 3617-3625
    • Elder, J.1    Kirschner, K.2
  • 33
    • 0022381731 scopus 로고
    • Bacterial luciferase: Demonstration of a catalytically competent altered conformational state following single turnover
    • AbouKhair, N. K., Ziegler, M. M., and Baldwin, T. O. (1985) Bacterial luciferase: demonstration of a catalytically competent altered conformational state following single turnover. Biochemistry 24, 3942-3947.
    • (1985) Biochemistry , vol.24 , pp. 3942-3947
    • AbouKhair, N.K.1    Ziegler, M.M.2    Baldwin, T.O.3
  • 34
    • 0003388018 scopus 로고
    • Electrostatic interactions
    • McGraw-Hill Book Co., New York
    • Jencks, W. P. (1969) Electrostatic Interactions, in Catalysis in Chemistry and Enzymology, pp 351-375, McGraw-Hill Book Co., New York.
    • (1969) Catalysis in Chemistry and Enzymology , pp. 351-375
    • Jencks, W.P.1
  • 35
    • 0022147096 scopus 로고
    • The Hofmeister effect and the behaviour of water at interfaces
    • Collins, K. D., and Washabaugh, M. W. (1985) The Hofmeister effect and the behaviour of water at interfaces. Quantum Rev. Biophys. 4, 323-422.
    • (1985) Quantum Rev. Biophys. , vol.4 , pp. 323-422
    • Collins, K.D.1    Washabaugh, M.W.2
  • 36
    • 0029792830 scopus 로고    scopus 로고
    • How Hofmeister ion interactions affect protein stability
    • Baldwin, R. L. (1996) How Hofmeister ion interactions affect protein stability. Biophys. J. 71, 2056-2063.
    • (1996) Biophys. J. , vol.71 , pp. 2056-2063
    • Baldwin, R.L.1
  • 37
    • 0025195499 scopus 로고
    • Mechanism of acid-induced folding of proteins
    • Goto, Y., Takahashi, N., and Fink, A. (1990) Mechanism of acid-induced folding of proteins. Biochemistry 29, 3480-3488.
    • (1990) Biochemistry , vol.29 , pp. 3480-3488
    • Goto, Y.1    Takahashi, N.2    Fink, A.3
  • 38
    • 0032512877 scopus 로고    scopus 로고
    • Linkage of protonation and anion binding to the folding of Sac7d
    • McCrary, B. S., Bedell, J., Edmondson, S. P., and Shriver, J. W. (1998) Linkage of protonation and anion binding to the folding of Sac7d. J. Mol. Biol. 276, 203-224.
    • (1998) J. Mol. Biol. , vol.276 , pp. 203-224
    • McCrary, B.S.1    Bedell, J.2    Edmondson, S.P.3    Shriver, J.W.4
  • 39
    • 0034237709 scopus 로고    scopus 로고
    • Anion-induced stabilization of human serum albumin prevents the formation of intermediate during urea denaturation
    • Muzammil, S., Kumar, Y., and Tayyab, S. (2000) Anion-induced stabilization of human serum albumin prevents the formation of intermediate during urea denaturation. Proteins: Struct., Funct., Genet. 40, 29-38.
    • (2000) Proteins: Struct., Funct., Genet. , vol.40 , pp. 29-38
    • Muzammil, S.1    Kumar, Y.2    Tayyab, S.3
  • 40
    • 0035814889 scopus 로고    scopus 로고
    • Linked folding and anion binding of the Bacillus subtilis ribonuclease P protein
    • Henkels, C. H., Kurz, J. C., Fierke, C. A., and Oas, T. G. (2001) Linked folding and anion binding of the Bacillus subtilis ribonuclease P protein. Biochemistry 40, 2777-2789.
    • (2001) Biochemistry , vol.40 , pp. 2777-2789
    • Henkels, C.H.1    Kurz, J.C.2    Fierke, C.A.3    Oas, T.G.4
  • 41
    • 0023375317 scopus 로고
    • Metal-dependent folding of a single zinc finger from transcription factor IIIA
    • Frankel, A. D., Berg, J., and Pabo, C. O. (1987) Metal-dependent folding of a single zinc finger from transcription factor IIIA. Proc. Natl. Acad. Sci. U.S.A. 84, 4841-4845.
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 4841-4845
    • Frankel, A.D.1    Berg, J.2    Pabo, C.O.3
  • 43
    • 0024276805 scopus 로고
    • Ribonuclease T1 is stabilized by cation and anion binding
    • Pace, C. N., and Grimsley, G. R. (1988) Ribonuclease T1 is stabilized by cation and anion binding. Biochemistry 27, 3242-3246.
    • (1988) Biochemistry , vol.27 , pp. 3242-3246
    • Pace, C.N.1    Grimsley, G.R.2
  • 45
    • 0015246307 scopus 로고
    • Stabilization of dihydrofolate reductase by inhibitors in vivo and in vitro
    • Hillcoat, B. L., Marshall, L., Gauldie, J., and Hiebert, M. (1971) Stabilization of dihydrofolate reductase by inhibitors in vivo and in vitro. Ann. N.Y. Acad. Sci. 186, 187-208.
    • (1971) Ann. N.Y. Acad. Sci. , vol.186 , pp. 187-208
    • Hillcoat, B.L.1    Marshall, L.2    Gauldie, J.3    Hiebert, M.4
  • 46
    • 0034649231 scopus 로고    scopus 로고
    • Use of domain specific ligands to study urea-induced unfolding of bovine serum albumin
    • Tayyab, S., Sharma, N., and Khan, M. M. (2000) Use of domain specific ligands to study urea-induced unfolding of bovine serum albumin. Biochem. Biophys. Res. Commun. 227, 83-88.
    • (2000) Biochem. Biophys. Res. Commun. , vol.227 , pp. 83-88
    • Tayyab, S.1    Sharma, N.2    Khan, M.M.3
  • 47
    • 0033837859 scopus 로고    scopus 로고
    • Ligand binding and thermodynamic stability of a multidomain protein, calmodulin
    • Masino, L., Martin, S. R., and Bayley, P. M. (2000) Ligand binding and thermodynamic stability of a multidomain protein, calmodulin. Protein Sci. 9, 1519-1529.
    • (2000) Protein Sci. , vol.9 , pp. 1519-1529
    • Masino, L.1    Martin, S.R.2    Bayley, P.M.3
  • 48
    • 0037085299 scopus 로고    scopus 로고
    • Effect of metal binding on the structural stability of pigeon liver malic enzyme
    • Chang, H. C., Chou, W. Y., and Chang, G. G. (2002) Effect of metal binding on the structural stability of pigeon liver malic enzyme. J. Biol. Chem. 277, 4663-4671.
    • (2002) J. Biol. Chem. , vol.277 , pp. 4663-4671
    • Chang, H.C.1    Chou, W.Y.2    Chang, G.G.3
  • 49
    • 0037066088 scopus 로고    scopus 로고
    • The two-domain NK1 fragment of plasminogen: Folding, ligand binding, and thermal stability profile
    • Douglas, J. T., von Haller, P. D., Gehrman, M., Llinas, M., and Schaller, J. (2002) The two-domain NK1 fragment of plasminogen: folding, ligand binding, and thermal stability profile. Biochemistry 41, 3302-3310.
    • (2002) Biochemistry , vol.41 , pp. 3302-3310
    • Douglas, J.T.1    Von Haller, P.D.2    Gehrman, M.3    Llinas, M.4    Schaller, J.5
  • 50
    • 0019883139 scopus 로고
    • Urea-induced unfolding of the alpha subunit of tryptophan synthase: Evidence for a multistate process
    • Matthews, C. R., and Crisanti, M. M. (1981) Urea-induced unfolding of the alpha subunit of tryptophan synthase: evidence for a multistate process. Biochemistry 20, 784-792.
    • (1981) Biochemistry , vol.20 , pp. 784-792
    • Matthews, C.R.1    Crisanti, M.M.2
  • 51
    • 0037540410 scopus 로고    scopus 로고
    • Nonsequential unfolding of the α/β barrel protein indole-3-glycerol-phosphate synthase
    • Sánchez del Pino, M. M., and Fersht, A. R. (1997) Nonsequential unfolding of the α/β barrel protein indole-3-glycerol-phosphate synthase. Biochemistry 36, 5560-5565.
    • (1997) Biochemistry , vol.36 , pp. 5560-5565
    • Sánchez del Pino, M.M.1    Fersht, A.R.2
  • 52
    • 0032813944 scopus 로고    scopus 로고
    • The progressive development of structure and stability during equilibrium folding of the α subunit of tryptophan synthase from Escherichia coli
    • Gualfetti, P. J., Bisel, O., and Matthews, C. R. (1999) The progressive development of structure and stability during equilibrium folding of the α subunit of tryptophan synthase from Escherichia coli. Protein Sci. 8, 1623-1635.
    • (1999) Protein Sci. , vol.8 , pp. 1623-1635
    • Gualfetti, P.J.1    Bisel, O.2    Matthews, C.R.3
  • 54
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.