Contribution of the multi-turn segment in the reversible thermal stability of hyperthermophile rubredoxin: NMR thermal chemical exchange analysis of sequence hybrids

Biophysical Chemistry

Volumn 116, Issue 1, 2005, Pages 57-65

  LeMaster, David M ^a   Tang, Jianzhong ^a   Paredes, Diana I ^a   Hernández, Griselda ^a  

^a STATE UNIVERSITY OF NEW YORK   (United States)

Author keywords

Differential thermostability; NMR chemical exchange; Reversible unfolding; Rubredoxin

Indexed keywords

HYBRID PROTEIN; RUBREDOXIN;

ARTICLE; CLOSTRIDIUM PASTEURIANUM; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN STABILITY; PYROCOCCUS FURIOSUS; TEMPERATURE SENSITIVITY; THERMODYNAMICS; THERMOSTABILITY; TRANSITION TEMPERATURE;

AMINO ACID SEQUENCE; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; RUBREDOXINS; TEMPERATURE; THERMODYNAMICS; ZINC;

CLOSTRIDIUM PASTEURIANUM; PYROCOCCUS FURIOSUS;

EID: 19444381342     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2005.01.010     Document Type: Article

References (36)

1. D. Wassenberg, C. Welker, and R. Jaenicke Thermodynamics of the unfolding of the cold-shock protein from Thermotoga maritima J. Mol. Biol. 289 1999 187 193
2. T. Dams, and R. Jaenicke Stability and folding of dihydrofolate reductase from the hyperthermophilic bacterium Thermotoga maritima Biochemistry 38 1999 9169 9178
3. W.A. Deutschman, and F.W. Dahlquist Thermodynamic basis for the increased thermostability of CheY from the hyperthermophile Thermotoga maritima Biochemistry 40 2001 13107 13113
4. J.H.G. Lebbink, V. Consalvi, R. Chiaraluce, K.D. Berndt, and R. Ladenstein Structural and thermodynamic studies on a salt-bridge triad in the NADP-binding domain of glutamate dehydrogenase from Thermotoga maritima: cooperativity and electrostatic contribution to stability Biochemistry 41 2002 15524 15535
5. E. Mombelli, M. Afshar, P. Fusi, M. Mariani, P. Tortora, J.P. Connelly, and R. Lange The role of phenylalanine 31 in maintaining the conformational stability of ribonuclease P2 from Sulfolobus solfataricus under extreme conditions of temperature and pressure Biochemistry 36 1997 8733 8742
6. A.T. Clark, B.S. McCrary, S.P. Edmondson, and J.W. Shriver Thermodynamics of core hydrophobicity and packing in the hyperthermophile protein Sac7d and Sso7d Biochemistry 43 2004 2840 2853
7. D.M. LeMaster, J. Tang, and G. Hernández Absence of kinetic thermal stabilization in a hyperthermophile rubredoxin indicated by 40 microsecond folding in the presence of irreversible denaturation Proteins 57 2004 118 127
8. R. Hiller, Z.H. Zhou, M.W.W. Adams, and S.W. Englander Stability and dynamics in a hyperthermophilic protein with melting temperature close to 200 degrees C Proc. Natl. Acad. Sci. U. S. A. 94 1997 11329 11332
9. G. Hernández, and D.M. LeMaster Reduced temperature dependence of collective conformational opening in a hyperthermophile rubredoxin Biochemistry 40 2001 14384 14391
10. S. Cavagnero, Z.H. Zhou, M.W.W. Adams, and S.I. Chan Response of rubredoxin from Pyrococcus furiosus to environmental changes: implications for the origin of hyperthermostability Biochemistry 34 1995 9865 9873
11. M.K. Eidsness, K.A. Richie, A.E. Burden, D.M. Kurtz, and R.A. Scott Dissecting contributions to the thermostability of Pyrococcus furiosus rubredoxin: beta-sheet chimeras Biochemistry 36 1997 10406 10413
12. S. Cavagnero, Z.H. Zhou, M.W.W. Adams, and S.I. Chan Unfolding mechanism of rubredoxin from Pyrococcus furiosus Biochemistry 37 1998 3377 3385
13. C.M. Bougault, M.K. Eidsness, and J.H. Prestegard Hydrogen bonds in rubredoxins from mesophilic and hyperthermophilic organisms Biochemistry 42 2003 4357 4372
14. D.H. Jung, N.S. Kang, and M.S. Jhon Site-directed mutation study on hyperthermostability of rubredoxin from Pyrococcus furiosus using molecular dynamics simulations in solution J. Phys. Chem., A 101 1997 466 471
15. K.D. Watenpaugh, L.C. Sieker, and L.H. Jensen The structure of rubredoxin at 1.2 Å resolution J. Mol. Biol. 131 1979 509 522
16. T. Lazaridis, I. Lee, and M. Karplus Dynamics and unfolding pathways of a hyperthermophilic and a mesophilic rubredoxin Protein Sci. 6 1997 2589 2605
17. P. Lamosa, A. Burke, R. Peist, R. Huber, M.Y. Liu, G. Silva, C. Rodrigues-Pousada, J. LeGall, C. Maycock, and H. Santos Thermostabilization of proteins by diglycerol phosphate, a new compatible solute from the hyperthermophile Archaeoglobus fulgidus Appl. Environ. Microbiol. 66 2000 1974 1979
18. L.C. Sieker, R.E. Stenkamp, L.H. Jensen, B. Prickril, and J. LeGall Structure of rubredoxin from the bacterium Desulfovibrio desulfuricans FEBS Lett. 208 1986 73 76
19. G.S. Huang, and T.G. Oas Submillisecond folding of monomeric λ repressor Proc. Natl. Acad. Sci. U. S. A. 92 1995 6878 6882
20. R.E. Burton, G.S. Huang, M.A. Daughterty, P.W. Fullbright, and T.G. Oas Microsecond protein folding through a compact transition state J. Mol. Biol. 263 1996 311 322
21. J.K. Myers, and T.G. Oas Preorganized secondary structure as an important determinant of fast protein folding Nat. Struct. Biol. 8 2001 552 558
22. J.K. Myers, and T.G. Oas Mechanisms of fast protein folding Annu. Rev. Biochem. 71 2002 783 815
23. U. Mayor, N.R. Guydosh, C.M. Johnson, J.G. Grossmann, S. Sato, G.S. Jas, S.M.V. Freund, D.O.V. Alonso, V. Daggett, and A.R. Fersht The complete folding pathway of a protein from nanoseconds to microseconds Nature 421 2003 863 867
24. D.D. Moore V.B. Chandra Current protocols in molecular biology vol. 1 1994 John Wiley & Sons New York 8.2.8 8.2.13
25. J. Tang, G. Hernández, and D.M. LeMaster Increased peptide deformylase activity for the N-formylmethionine processing of proteins overexpressed in Escherichia coli: application to homogeneous rubredoxin production Protein Expr. Purif. 36 2004 100 105
26. 2H labeled proteins J. Biomol. NMR 13 1999 369 374
27. 1H-NMR parameters of common amino acid residues measured in aqueous solutions of the linear tetrapeptides Gly-Gly-X-Ala at pressures between 0.1 and 200 MPa Biophys. Chemist. 96 2002 129 140
28. S. Cavagnero, D.A. Debe, Z.H. Zhou, M.W.W. Adams, and S.I. Chan Kinetic role of electrostatic interactions in the unfolding of hyperthermophilic and mesophilic rubredoxins Biochemistry 37 1998 3369 3376
29. J.K. Myers, C.N. Pace, and J.M. Scholtz Denaturant m values and heat-capacity changes: relation to changes in accessible surface areas of protein folding Protein Sci. 4 1995 2138 2148
30. W.J. Becktel, and J.A. Schellman Protein stability curves Biopolymers 26 1987 1859 1877
31. T. Chatake, K. Kurihara, I. Tanaka, I. Tsyba, R. Bau, F.E. Jenney, M.W.W. Adams, and N. Niimura A neutron crystallographic analysis of a rubredoxin mutant at 1.6 Å resolution Acta Crystallogr., D Biol. Crystallogr. 60 2004 1364 1373
32. K.W. Plaxco, K.T. Simons, and D. Baker Contact order, transition state placement and the refolding rates of single domain proteins J. Mol. Biol. 277 1998 985 994
33. G. Hernández, F.E. Jenney, M.W.W. Adams, and D.M. LeMaster Millisecond time scale conformational flexibility in a hyperthermophile protein at ambient temperature Proc. Natl. Acad. Sci. U. S. A. 97 2000 3166 3170
34. K.D. Watenpaugh, L.C. Sieker, and L.H. Jensen Crystallographic refinement of rubredoxin at 1.2 Å resolution J. Mol. Biol. 138 1980 615 633
35. R. Bau, D.C. Rees, D.M. Kurtz, R.A. Scott, H.S. Huang, M.W.W. Adams, and M.K. Eidsness Crystal-structure of rubredoxin from Pyrococcus furiosus at 0.95 angstrom resolution, and the structures of N-terminal methionine and formylmethionine variants of Pf Rd. Contributions of N-terminal interactions to thermostability J. Biol. Inorg. Chem. 3 1998 484 493
36. B. Lee, and F.M. Richards The interpretation of protein structures: estimation of static accessibility J. Mol. Biol. 55 1971 379 400