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Volumn 385, Issue 5, 2009, Pages 1590-1599

Coupling of Domain Swapping to Kinetic Stability in a Thioredoxin Mutant

Author keywords

domain swapping; DSC; evolution; kinetic and thermodynamic stability; X ray protein structure

Indexed keywords

THIOREDOXIN;

EID: 58549113633     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.11.040     Document Type: Article
Times cited : (20)

References (49)
  • 1
    • 0036108484 scopus 로고    scopus 로고
    • 3D domain swapping: as domains continue to swap
    • Liu Y., and Eisenberg D. 3D domain swapping: as domains continue to swap. Protein Sci. 11 (2002) 1285-1299
    • (2002) Protein Sci. , vol.11 , pp. 1285-1299
    • Liu, Y.1    Eisenberg, D.2
  • 2
    • 0030770294 scopus 로고    scopus 로고
    • Oligomer formation by 3D domain swapping: a model for protein assembly and misassembly
    • Schlunegger M.P., Bennett M.J., and Eisenberg D. Oligomer formation by 3D domain swapping: a model for protein assembly and misassembly. Adv. Protein Chem. 50 (1997) 61-122
    • (1997) Adv. Protein Chem. , vol.50 , pp. 61-122
    • Schlunegger, M.P.1    Bennett, M.J.2    Eisenberg, D.3
  • 3
    • 0028865843 scopus 로고
    • 3D domain swapping: a mechanism for oligomer assembly
    • Bennett M.J., Schlunegger M.P., and Eisenberg D. 3D domain swapping: a mechanism for oligomer assembly. Protein Sci. 4 (1995) 2455-2468
    • (1995) Protein Sci. , vol.4 , pp. 2455-2468
    • Bennett, M.J.1    Schlunegger, M.P.2    Eisenberg, D.3
  • 4
    • 0035826713 scopus 로고    scopus 로고
    • Three-dimensional domain swapping in p13suc1 occurs in the unfolded state and is controlled by conserved proline residues
    • Rousseau F., Schymkowitz J.W., Wilkinson H.R., and Itzhaki L.S. Three-dimensional domain swapping in p13suc1 occurs in the unfolded state and is controlled by conserved proline residues. Proc. Natl Acad. Sci. USA 98 (2001) 5596-5601
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 5596-5601
    • Rousseau, F.1    Schymkowitz, J.W.2    Wilkinson, H.R.3    Itzhaki, L.S.4
  • 5
    • 0028077637 scopus 로고
    • Refined structure of dimeric diphtheria toxin at 2.0 Å resolution
    • Bennett M.J., Choe S., and Eisenberg D. Refined structure of dimeric diphtheria toxin at 2.0 Å resolution. Protein Sci. 3 (1994) 1444-1463
    • (1994) Protein Sci. , vol.3 , pp. 1444-1463
    • Bennett, M.J.1    Choe, S.2    Eisenberg, D.3
  • 7
    • 0037102362 scopus 로고    scopus 로고
    • Getting out of shape
    • Dobson C.M. Getting out of shape. Nature 418 (2002) 729-730
    • (2002) Nature , vol.418 , pp. 729-730
    • Dobson, C.M.1
  • 8
    • 39349110541 scopus 로고    scopus 로고
    • Molecular mechanisms of polypeptide aggregation in human diseases
    • Khare S.D., and Dokholyan N.V. Molecular mechanisms of polypeptide aggregation in human diseases. Curr. Protein Pept. Sci. 8 (2007) 573-579
    • (2007) Curr. Protein Pept. Sci. , vol.8 , pp. 573-579
    • Khare, S.D.1    Dokholyan, N.V.2
  • 10
    • 34249654016 scopus 로고    scopus 로고
    • Thioredoxin suppresses Parkin-associated endothelin receptor-like receptor-induced neurotoxicity and extends longevity in Drosophila
    • Umeda-Kameyama Y., Tsuda M., Ohkura C., Matsuo T., Namba Y., Ohuchi Y., and Aigaki T. Thioredoxin suppresses Parkin-associated endothelin receptor-like receptor-induced neurotoxicity and extends longevity in Drosophila. J. Biol. Chem. 282 (2007) 11180-11187
    • (2007) J. Biol. Chem. , vol.282 , pp. 11180-11187
    • Umeda-Kameyama, Y.1    Tsuda, M.2    Ohkura, C.3    Matsuo, T.4    Namba, Y.5    Ohuchi, Y.6    Aigaki, T.7
  • 12
    • 0029165589 scopus 로고
    • Thioredoxin-a fold for all reasons
    • Martin J.L. Thioredoxin-a fold for all reasons. Structure 3 (1995) 245-250
    • (1995) Structure , vol.3 , pp. 245-250
    • Martin, J.L.1
  • 13
    • 33645881071 scopus 로고    scopus 로고
    • Pathways of disulfide bond formation in Escherichia coli
    • Messens J., and Collet J.F. Pathways of disulfide bond formation in Escherichia coli. Int. J. Biochem. Cell Biol. 38 (2006) 1050-1062
    • (2006) Int. J. Biochem. Cell Biol. , vol.38 , pp. 1050-1062
    • Messens, J.1    Collet, J.F.2
  • 14
    • 33749364627 scopus 로고    scopus 로고
    • The origami of thioredoxin-like folds
    • Pan J.L., and Bardwell J.C. The origami of thioredoxin-like folds. Protein Sci. 15 (2006) 2217-2227
    • (2006) Protein Sci. , vol.15 , pp. 2217-2227
    • Pan, J.L.1    Bardwell, J.C.2
  • 16
    • 2442491135 scopus 로고    scopus 로고
    • NrdH-redoxin of Corynebacterium ammoniagenes forms a domain-swapped dimer
    • Stehr M., and Lindqvist Y. NrdH-redoxin of Corynebacterium ammoniagenes forms a domain-swapped dimer. Proteins 55 (2004) 613-619
    • (2004) Proteins , vol.55 , pp. 613-619
    • Stehr, M.1    Lindqvist, Y.2
  • 17
    • 34047142083 scopus 로고    scopus 로고
    • The conserved active site proline determines the reducing power of Staphylococcus aureus thioredoxin
    • Roos G., Garcia-Pino A., Van Belle K., Brosens E., Wahni K., Vandenbussche G., et al. The conserved active site proline determines the reducing power of Staphylococcus aureus thioredoxin. J. Mol. Biol. 368 (2007) 800-811
    • (2007) J. Mol. Biol. , vol.368 , pp. 800-811
    • Roos, G.1    Garcia-Pino, A.2    Van Belle, K.3    Brosens, E.4    Wahni, K.5    Vandenbussche, G.6
  • 18
    • 0030726361 scopus 로고    scopus 로고
    • pH and temperature-induced molten globule-like denatured states of equinatoxin II: a study by UV-melting, DSC, far- and near-UV CD spectroscopy, and ANS fluorescence
    • Poklar N., Lah J., Salobir M., Macek P., and Vesnaver G. pH and temperature-induced molten globule-like denatured states of equinatoxin II: a study by UV-melting, DSC, far- and near-UV CD spectroscopy, and ANS fluorescence. Biochemistry 36 (1997) 14345-14352
    • (1997) Biochemistry , vol.36 , pp. 14345-14352
    • Poklar, N.1    Lah, J.2    Salobir, M.3    Macek, P.4    Vesnaver, G.5
  • 19
    • 0026586591 scopus 로고
    • Theoretical analysis of Lumry-Eyring models in differential scanning calorimetry
    • Sanchez-Ruiz J.M. Theoretical analysis of Lumry-Eyring models in differential scanning calorimetry. Biophys. J. 61 (1992) 921-935
    • (1992) Biophys. J. , vol.61 , pp. 921-935
    • Sanchez-Ruiz, J.M.1
  • 20
    • 0025883245 scopus 로고
    • Structural and functional relations among thioredoxins of different species
    • Eklund H., Gleason F.K., and Holmgren A. Structural and functional relations among thioredoxins of different species. Proteins 11 (1991) 13-28
    • (1991) Proteins , vol.11 , pp. 13-28
    • Eklund, H.1    Gleason, F.K.2    Holmgren, A.3
  • 21
    • 0033592956 scopus 로고    scopus 로고
    • The essential catalytic redox couple in arsenate reductase from Staphylococcus aureus
    • Messens J., Hayburn G., Desmyter A., Laus G., and Wyns L. The essential catalytic redox couple in arsenate reductase from Staphylococcus aureus. Biochemistry 38 (1999) 16857-16865
    • (1999) Biochemistry , vol.38 , pp. 16857-16865
    • Messens, J.1    Hayburn, G.2    Desmyter, A.3    Laus, G.4    Wyns, L.5
  • 23
    • 41449117607 scopus 로고    scopus 로고
    • Thioredoxins and glutaredoxins as facilitators of protein folding
    • Berndt C., Lillig C.H., and Holmgren A. Thioredoxins and glutaredoxins as facilitators of protein folding. Biochim. Biophys. Acta 1783 (2008) 641-650
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 641-650
    • Berndt, C.1    Lillig, C.H.2    Holmgren, A.3
  • 24
    • 0038245262 scopus 로고    scopus 로고
    • Chaperone properties of Escherichia coli thioredoxin and thioredoxin reductase
    • Kern R., Malki A., Holmgren A., and Richarme G. Chaperone properties of Escherichia coli thioredoxin and thioredoxin reductase. Biochem. J. 371 (2003) 965-972
    • (2003) Biochem. J. , vol.371 , pp. 965-972
    • Kern, R.1    Malki, A.2    Holmgren, A.3    Richarme, G.4
  • 25
    • 0039714219 scopus 로고    scopus 로고
    • Characterization of Escherichia coli thioredoxin variants mimicking the active-sites of other thiol/disulfide oxidoreductases
    • Mossner E., Huber-Wunderlich M., and Glockshuber R. Characterization of Escherichia coli thioredoxin variants mimicking the active-sites of other thiol/disulfide oxidoreductases. Protein Sci. 7 (1998) 1233-1244
    • (1998) Protein Sci. , vol.7 , pp. 1233-1244
    • Mossner, E.1    Huber-Wunderlich, M.2    Glockshuber, R.3
  • 27
    • 0025865875 scopus 로고
    • Substitution of the conserved tryptophan 31 in Escherichia coli thioredoxin by site-directed mutagenesis and structure-function analysis
    • Krause G., and Holmgren A. Substitution of the conserved tryptophan 31 in Escherichia coli thioredoxin by site-directed mutagenesis and structure-function analysis. J. Biol. Chem. 266 (1991) 4056-4066
    • (1991) J. Biol. Chem. , vol.266 , pp. 4056-4066
    • Krause, G.1    Holmgren, A.2
  • 28
    • 33644759558 scopus 로고    scopus 로고
    • Thioredoxin fusions increase folding of single chain Fv antibodies in the cytoplasm of Escherichia coli: evidence that chaperone activity is the prime effect of thioredoxin
    • Jurado P., de Lorenzo V., and Fernandez L.A. Thioredoxin fusions increase folding of single chain Fv antibodies in the cytoplasm of Escherichia coli: evidence that chaperone activity is the prime effect of thioredoxin. J. Mol. Biol. 357 (2006) 49-61
    • (2006) J. Mol. Biol. , vol.357 , pp. 49-61
    • Jurado, P.1    de Lorenzo, V.2    Fernandez, L.A.3
  • 31
    • 33645951646 scopus 로고    scopus 로고
    • The Escherichia coli thioredoxin homolog YbbN/Trxsc is a chaperone and a weak protein oxidoreductase
    • Caldas T., Malki A., Kern R., Abdallah J., and Richarme G. The Escherichia coli thioredoxin homolog YbbN/Trxsc is a chaperone and a weak protein oxidoreductase. Biochem. Biophys. Res. Commun. 343 (2006) 780-786
    • (2006) Biochem. Biophys. Res. Commun. , vol.343 , pp. 780-786
    • Caldas, T.1    Malki, A.2    Kern, R.3    Abdallah, J.4    Richarme, G.5
  • 32
    • 0035832893 scopus 로고    scopus 로고
    • Studies on the function of yeast protein disulfide isomerase in renaturation of proteins
    • Katiyar S., Till E.A., and Lennarz W.J. Studies on the function of yeast protein disulfide isomerase in renaturation of proteins. Biochim. Biophys. Acta 1548 (2001) 47-56
    • (2001) Biochim. Biophys. Acta , vol.1548 , pp. 47-56
    • Katiyar, S.1    Till, E.A.2    Lennarz, W.J.3
  • 33
    • 0031913197 scopus 로고    scopus 로고
    • Mechanism and evolution of protein dimerization
    • Xu D., Tsai C.J., and Nussinov R. Mechanism and evolution of protein dimerization. Protein Sci. 7 (1998) 533-544
    • (1998) Protein Sci. , vol.7 , pp. 533-544
    • Xu, D.1    Tsai, C.J.2    Nussinov, R.3
  • 34
    • 38349091102 scopus 로고    scopus 로고
    • The buried diversity of bovine seminal ribonuclease: shape and cytotoxicity of the swapped non-covalent form of the enzyme
    • Merlino A., Ercole C., Picone D., Pizzo E., Mazzarella L., and Sica F. The buried diversity of bovine seminal ribonuclease: shape and cytotoxicity of the swapped non-covalent form of the enzyme. J. Mol. Biol. 376 (2008) 427-437
    • (2008) J. Mol. Biol. , vol.376 , pp. 427-437
    • Merlino, A.1    Ercole, C.2    Picone, D.3    Pizzo, E.4    Mazzarella, L.5    Sica, F.6
  • 36
    • 37249067732 scopus 로고    scopus 로고
    • The origin of protein interactions and allostery in colocalization
    • Kuriyan J., and Eisenberg D. The origin of protein interactions and allostery in colocalization. Nature 450 (2007) 983-990
    • (2007) Nature , vol.450 , pp. 983-990
    • Kuriyan, J.1    Eisenberg, D.2
  • 37
    • 0037122769 scopus 로고    scopus 로고
    • Energetic landscape of alpha-lytic protease optimizes longevity through kinetic stability
    • Jaswal S.S., Sohl J.L., Davis J.H., and Agard D.A. Energetic landscape of alpha-lytic protease optimizes longevity through kinetic stability. Nature 415 (2002) 343-346
    • (2002) Nature , vol.415 , pp. 343-346
    • Jaswal, S.S.1    Sohl, J.L.2    Davis, J.H.3    Agard, D.A.4
  • 38
    • 14644412777 scopus 로고    scopus 로고
    • Comprehensive analysis of protein folding activation thermodynamics reveals a universal behavior violated by kinetically stable proteases
    • Jaswal S.S., Truhlar S.M., Dill K.A., and Agard D.A. Comprehensive analysis of protein folding activation thermodynamics reveals a universal behavior violated by kinetically stable proteases. J. Mol. Biol. 347 (2005) 355-366
    • (2005) J. Mol. Biol. , vol.347 , pp. 355-366
    • Jaswal, S.S.1    Truhlar, S.M.2    Dill, K.A.3    Agard, D.A.4
  • 39
    • 0035801540 scopus 로고    scopus 로고
    • Three-dimensional domain swapping in the folded and molten-globule states of cystatins, an amyloid-forming structural superfamily
    • Staniforth R.A., Giannini S., Higgins L.D., Conroy M.J., Hounslow A.M., Jerala R., et al. Three-dimensional domain swapping in the folded and molten-globule states of cystatins, an amyloid-forming structural superfamily. EMBO J. 20 (2001) 4774-4781
    • (2001) EMBO J. , vol.20 , pp. 4774-4781
    • Staniforth, R.A.1    Giannini, S.2    Higgins, L.D.3    Conroy, M.J.4    Hounslow, A.M.5    Jerala, R.6
  • 42
    • 0027062923 scopus 로고
    • Renaturation of citrate synthase: influence of denaturant and folding assistants
    • Zhi W., Landry S.J., Gierasch L.M., and Srere P.A. Renaturation of citrate synthase: influence of denaturant and folding assistants. Protein Sci. 1 (1992) 522-529
    • (1992) Protein Sci. , vol.1 , pp. 522-529
    • Zhi, W.1    Landry, S.J.2    Gierasch, L.M.3    Srere, P.A.4
  • 43
    • 0026206788 scopus 로고
    • Sparse matrix sampling: a screening method for crystallization of proteins
    • Jancarik J., and Kim S.-H. Sparse matrix sampling: a screening method for crystallization of proteins. J. Appl. Crystallogr. 24 (1991) 409-411
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 409-411
    • Jancarik, J.1    Kim, S.-H.2
  • 44
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 45
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project, No. 4
    • Collaborative Computational Project, No. 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr., Sect. D: Biol. Crystallogr. 50 (1994) 760-763
    • (1994) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.50 , pp. 760-763
  • 46
    • 33846426122 scopus 로고    scopus 로고
    • Solving structures of protein complexes by molecular replacement with Phaser
    • McCoy A.J. Solving structures of protein complexes by molecular replacement with Phaser. Acta Crystallogr., Sect. D: Biol. Crystallogr. 63 (2007) 32-41
    • (2007) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.63 , pp. 32-41
    • McCoy, A.J.1


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