Identification of an active dimeric intermediate populated during the unfolding process of the cambialistic superoxide dismutase from Streptococcus mutans

Biochimie

Volumn 94, Issue 3, 2012, Pages 768-775

  Merlino, Antonello ^a,b   Russo Krauss, Irene ^a   Rossi, Bianca ^a   Vergara, Alessandro ^a,b   De Vendittis, Alberto ^a   Marco, Salvatore ^a   De Vendittis, Emmanuele ^a   Sica, Filomena ^a,b  

^a UNIVERSITY OF NAPLES FEDERICO II   (Italy)

^b CNR   (Italy)

Author keywords

Chemical stability; Dimeric intermediate; Superoxide dismutase; Thermal stability; Unfolding

Indexed keywords

DIMER; GUANIDINE; SUPEROXIDE DISMUTASE;

ARTICLE; CIRCULAR DICHROISM; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME DENATURATION; ENZYME STABILITY; ENZYME STRUCTURE; FLUORESCENCE ANALYSIS; MOLECULAR MODEL; NONHUMAN; PROTEIN UNFOLDING; STREPTOCOCCUS MUTANS; STRUCTURE ANALYSIS; THERMOSTABILITY; ULTRAVIOLET SPECTROSCOPY;

BACTERIAL PROTEINS; CIRCULAR DICHROISM; PROTEIN FOLDING; STREPTOCOCCUS MUTANS; SUPEROXIDE DISMUTASE;

STREPTOCOCCUS MUTANS;

EID: 84857051056     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2011.11.008     Document Type: Article

References (40)

1. C.R. Matthews Pathway of protein folding Annu. Rev. Biochem. 62 1993 653 683
2. K.E. Neet, and D.E. Timm Conformational stability of dimeric proteins: quantitative studies by equilibrium denaturation Protein Sci. 3 1994 2167 2174
3. J.A. Rumfeldt, C. Galvagnion, K.A. Vassall, and E.M. Meiering Conformational stability and folding mechanisms of dimeric proteins Prog. Biophys. Mol. Biol. 98 2008 61 84
4. P.S. Kim, and R.L. Baldwin Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding Annu. Rev. Biochem. 51 1982 459 489
5. S.M. Doyle, E.H. Braswell, and C.M. Teschke SecA folds via a dimeric intermediate Biochemistry 39 2000 11667 11676
6. K. Bose, and A.C. Clark Dimeric procaspase-3 unfolds via a four-state equilibrium process Biochemistry 40 2001 14236 14242 (Pubitemid 33081627)
7. M.E. Chanez-Cardenas, G. Perez-Hernandez, B.G. Sanchez-Rebollar, M. Costas, and E. Vazquez-Contreras Reversible equilibrium unfolding of triosephosphate isomerase from Trypanosoma cruzi in guanidinium hydrochloride involves stable dimeric and monomeric intermediates Biochemistry 44 2005 10883 10892 (Pubitemid 41153649)
8. S. Gildenhuys, L.A. Wallace, J.P. Burke, D. Balchin, Y. Sayed, and H.W. Dirr Class Pi glutathione transferase unfolds via a dimeric and not monomeric intermediate: functional implications for an unstable monomer Biochemistry 49 2010 5074 5081
9. J.M. McCord, and I. Fridovich Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein) J. Biol. Chem. 244 1969 6049 6055
10. J.M. McCord, and I. Fridovich The utility of superoxide dismutase in studying free radical reactions. I. Radicals generated by the interaction of sulfite, dimethyl sulfoxide, and oxygen J. Biol. Chem. 244 1969 6056 6063
11. V.C. Culotta, M. Yang, and T.V. O'Halloran Activation of superoxide dismutases: putting the metal to the pedal Biochim. Biophys. Acta. 1763 2006 747 758 (Pubitemid 44189546)
12. A.F. Miller Superoxide dismutases: active sites that save, but a protein that kills Curr. Opin. Chem. Biol. 8 2004 162 168
13. W.C. Stallings, K.A. Pattridge, R.K. Strong, and M.L. Ludwig Manganese and iron superoxide dismutases are structural homologs J. Biol. Chem. 259 1984 10695 10699 (Pubitemid 14031192)
14. J.A. Rumfeldt, P.B. Stathopulos, A. Chakrabarrty, J.R. Lepock, and E.M. Meiering Mechanism and thermodynamics of guanidinium chloride-induced denaturation of ALS-associated mutant Cu, Zn superoxide dismutases J. Mol. Biol. 355 2006 106 123 (Pubitemid 41774143)
15. G. Mei, N. Rosato, N. Silva Jr., R. Rusch, E. Gratton, I. Savini, and A. Finazzi-Agro Denaturation of human Cu/Zn superoxide dismutase by guanidine hydrochloride: a dynamic fluorescence study Biochemistry 31 1992 7224 7230
16. M.E. Stroppolo, F. Malvezzi-Campeggi, G. Mei, N. Rosato, and A. Desideri Role of the tertiary and quaternary structures in the stability of dimeric copper, zinc superoxide dismutases Arch. Biochem. Biophys. 377 2000 215 218 (Pubitemid 30331880)
17. A.F. Miller A. Messerschimdt, R. Huber, K. Wieghardt, T. Paulos, Handbook of Metalloproteins 2001 Wiley and Sons Chicester
18. M.E. Stroupe, M. Di Donato, and J.A. Tainer A. Messerschimdt, R. Huber, K. Wieghardt, T. Paulos, Handbook of Metalloproteins 2001 Wiley and Sons Chicester
19. S. Wang, W.F. Liu, Y.Z. He, A. Zhang, L. Huang, Z.Y. Dong, and Y.B. Yan Multistate folding of a hyperthermostable Fe-superoxide dismutase (TcSOD) in guanidinium hydrochloride: the importance of the quaternary structure Biochim. Biophys. Acta 1784 2008 445 454
20. H.L. Pedersen, N.P. Willassen, and I. Leiros The first structure of a cold-adapted superoxide dismutase (SOD): biochemical and structural characterization of iron SOD from Aliivibrio salmonicida Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 65 2009 84 92
21. A. Merlino, I. Russo Krauss, I. Castellano, E. De Vendittis, B. Rossi, M. Conte, A. Vergara, and F. Sica Structure and flexibility in cold-adapted iron superoxide dismutases: the case of the enzyme isolated from Pseudoalteromonas haloplanktis J. Struct. Biol. 172 2010 343 352
22. A. De Vendittis, M. Amato, A. Mickniewicz, G. Parlato, A. De Angelis, I. Castellano, R. Rullo, F. Riccitiello, S. Rengo, M. Masullo, and E. De Vendittis Regulation of the properties of superoxide dismutase from the dental pathogenic microorganism Streptococcus mutans by iron- and manganese-bound co-factor Mol. Biosyst. 6 2010 1973 1982
23. M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
24. A. Dello Russo, R. Rullo, G. Nitti, M. Masullo, and V. Bocchini Iron superoxide dismutase from the archaeon Sulfolobus solfataricus: average hydrophobicity and amino acid weight are involved in the adaptation of proteins to extreme environments Biochim. Biophys. Acta 1343 1997 23 30 (Pubitemid 28015476)
25. L. Whitmore, and B.A. Wallace DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data Nucleic Acids Res. 32 2004 W668 W673 (Pubitemid 38997420)
26. P. Liu, H.E. Ewis, Y.J. Huang, C.D. Lu, P.C. Tai, and I.T. Weber Structure of Bacillus subtilis superoxide dismutase Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 63 2007 1003 1007 (Pubitemid 350224335)
27. T.A. Jones, J.Y. Zou, S.W. Cowan, and M. Kjeldgaard Improved methods for building protein models in electron density maps and the location of errors in these models Acta Crystallogr. A 47 Pt 2 1991 110 119
28. D. Van Der Spoel, E. Lindahl, B. Hess, G. Groenhof, A.E. Mark, and H.J. Berendsen GROMACS: fast, flexible, and free J. Comput. Chem. 26 2005 1701 1718 (Pubitemid 43076182)
29. A. Merlino, L. Esposito, and L. Vitagliano Polyglutamine repeats and beta-helix structure: molecular dynamics study Proteins 63 2006 918 927 (Pubitemid 43765143)
30. M. Porcelli, M.A. Moretti, L. Concilio, S. Forte, A. Merlino, G. Graziano, and G. Cacciapuoti S-adenosylhomocysteine hydrolase from the archaeon Pyrococcus furiosus: biochemical characterization and analysis of protein structure by comparative molecular modeling Proteins 58 2005 815 825 (Pubitemid 40271246)
31. E. Pizzo, A. Merlino, M. Turano, I. Russo Krauss, F. Coscia, A. Zanfardino, M. Varcamonti, A. Furia, C. Giancola, L. Mazzarella, F. Sica, and G. D'Alessio A new RNase sheds light on the RNase/angiogenin subfamily from zebrafish Biochem. J. 433 2011 345 355
32. I. Castellano, A. Merlino, M. Rossi, and F. La Cara Biochemical and structural properties of gamma-glutamyl transpeptidase from Geobacillus thermodenitrificans: an enzyme specialized in hydrolase activity Biochimie 92 2010 464 474
33. I. Castellano, A. Di Salle, A. Merlino, M. Rossi, and F. La Cara Gene cloning and protein expression of gamma-glutamyltranspeptidases from Thermus thermophilus and Deinococcus radiodurans: comparison of molecular and structural properties with mesophilic counterparts Extremophiles 15 2011 259 270
34. M. Wiederstein, and M.J. Sippl ProSA-web: interactive web service for the recognition of errors in three-dimensional structures of proteins Nucleic Acids Res. 35 2007 W407 W410
35. E. Padros, A. Morros, J. Manosa, and M. Dunach The state of tyrosine and phenylalanine residues in proteins analyzed by fourth-derivative spectrophotometry. Histone H1 and ribonuclease A Eur. J. Biochem. 127 1982 117 122
36. M. Dunach, M. Sabes, and E. Padros Fourth-derivative spectrophotometry analysis of tryptophan environment in proteins. Application to melittin, cytochrome c and bacteriorhodopsin Eur. J. Biochem. 134 1983 123 128
37. S. Wang, Y. Yan, and Z. Dong Contributions of the C-terminal helix to the structural stability of a hyperthermophilic Fe-superoxide dismutase (TcSOD) Int. J. Mol. Sci. 10 2009 5498 5512
38. J.B. Cooper, S. Saward, P.T. Erskine, M.O. Badasso, S.P. Wood, Y. Zhang, and D. Young X-ray structure analysis of an engineered Fe-superoxide dismutase Gly-Ala mutant with significantly reduced stability to denaturant FEBS Lett. 387 1996 105 108 (Pubitemid 26178903)
39. H.C.K. Hsieh, C.C. Chiu, and C. Yu Equilibrium unfolding of a oligomeric protein involved the formation of multimeric intermediate state Biochem. Biophys. Res. Commun. 326 2005 108 114
40. B. Liujiao, Z. Than, Y. Xiaoyani, L. Li, and Z. Xiaohui Unfolding of bovine heart cytochrome c induced by urea and guanidine hydrochloride Chin. J. Chem. 29 2011 813 821