The Stability and Formation of Native Proteins from Unfolded Monomers Is Increased through Interactions with Unrelated Proteins

PLoS ONE

Volumn 2, Issue 6, 2007, Pages

  Rodríguez Almazán, Claudia ^a   Torner, Francisco J ^b   Costas, Miguel ^b   Pérez Montfort, Ruy ^a   de Gómez Puyou, Marieta Tuena ^a   Puyou, Armando Gómez ^a  

^a INSTITUTO DE FISIOLOGÍA CELULAR   (Mexico)

^b UNIVERSIDAD NACIONAL AUTÓNOMA DE MÉXICO   (Mexico)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN; RECOMBINANT PROTEIN; TRIOSEPHOSPHATE ISOMERASE;

ANIMAL; ARTICLE; CHEMISTRY; DIMERIZATION; ENZYMOLOGY; KINETICS; LEISHMANIA MEXICANA; METABOLISM; PROTEIN BINDING; PROTEIN FOLDING; SACCHAROMYCES CEREVISIAE; TRYPANOSOMA BRUCEI;

ANIMALS; DIMERIZATION; KINETICS; LEISHMANIA MEXICANA; PROTEIN BINDING; PROTEIN FOLDING; PROTEINS; RECOMBINANT PROTEINS; SACCHAROMYCES CEREVISIAE; TRIOSE-PHOSPHATE ISOMERASE; TRYPANOSOMA BRUCEI BRUCEI;

EID: 52649135840     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0000497     Document Type: Article

References (45)

1. Jaenicke R, Lilie H, (2000) Folding and association of oligomeric and multimeric proteins. Adv Protein Chem 53: 329-401.
2. Fedorov AN, Baldwin T, (1997) Cotranslational protein folding. J Biol Chem 272: 32715-32718.
3. Evans MS, Clarke IV TF, Clark PL, (2005) Conformations of co-translational folding intermediates. Prot Pept Lett 12: 189-195.
4. Zimmerman SB, Minton AP, (1993) Macromolecular crowding: biochemical, biophysical, and physiological consequences. Annu Rev Biophys Biomol Struct 22: 27-65.
5. Ellis RJ, (2001) Macromolecular crowding: obvious but underappreciated. Trends Biochem Sci 26: 59-604.
6. Minton AP, (2001) The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media. J Biol Chem 276: 10577-10580.
7. Hall D, Minton AP, (2003) Macromolecular crowding: qualitative and semi-quantitative, quantitative challenges. Biochem Biophys Acta 1649: 127-139.
8. Chebotareva NA, Kurganov BI, Livanova NB, (2004) Biochemical effects of molecular crowding. Biochemistry (Moscow) 69: 1239-1251.
9. Schellman JA, (1975) Macromolecular binding. Biopolymers 14: 999-1018.
10. McVittie JD, Esnouf MP, Peacocke AR, (1977) The denaturation-renaturation of chicken-muscle triosephosphate isomerase in guanidinium chloride. Eur J Biochem 81: 307-315.
11. Waley SG, (1973) Refolding of triosephosphate isomerase. Biochem J 135: 165-172.
12. Zabori S, Rudolph R, Jaenicke R, (1980) Folding and association of triosephosphate isomerase from rabbit muscle. Z Naturforsch [C] 35: 999-1004.
13. Nájera H, Costas M, Fernández-Velasco DA, (2003) Thermodynamic characterization of yeast triosephosphate isomerase refolding: insights into the interplay between function and stability as reasons for the oligomeric nature of the enzyme. Biochem J 370: 785-792.
14. Zomosa-Signoret V, Hernández-Alcántara G, Reyes-Vivas H, Martínez-Martínez E, Garza Ramos G, et al.(2003) Control of the reactivation kinetics of homodimeric triosephosphate isomerase from unfolded monomers. Biochemistry 42: 3311-3318.
15. Albery J, Knowles JR, (1976) Evolution of enzyme function and the development of catalytic efficiency. Biochemistry 15: 5631-5640.
16. Knowles JR, (1991) Enzyme catalysis: not different, just better. Nature 350: 121-124.
17. Xiang J, Jung JY, Sampson NS, (2004) Entropy effects on protein hinges: the reaction catalyzed by triosephosphate isomerase. Biochemistry 43: 11436-11445.
18. Williams JC, McDermott AE, (1995) Dynamics of the flexible loop of triosephosphate isomerase: the loop motion is not ligand gated. Biochemistry 34: 8309-8319.
19. van den Berg B, Wain R, Dobson CM, Ellis RJ, (2000) Macromolecular crowding perturbs protein refolding kinetics implications for folding inside the cell. EMBO J 19: 3870-3875.
20. Zhou B-R, Liang Y, Du F, Zhou Z, Chen J, (2004) Mixed macromolecular crowding accelerates the oxidative refolding of reduced, denatured lysozyme. J Biol Chem 279: 55109-55116.
21. Zhi W, Landry SJ, Gierasch LM, Srere PA, (1992) Renaturation of citrate synthase: influence of denaturant and folding assistants. Protein Sci 1: 522-529.
22. Ren G, Lin Z, Tsou C-L, Wang C-C, (2003) Effects of macromolecular crowding on the unfolding and the refolding of D-glyceraldehyde-3-phosphate dehydrogenase. J Prot Chem 22: 431-439.
23. Li J, Zhang S, Wang C-C, (2001) Effects of macromolecular crowding on the refolding of glucose-6-phosphate dehydrogenase and protein disulfide isomerase. J Biol Chem 276: 34396-34401.
24. Goloubinoff P, Gatenby AA, Lorimer GH, (1989) GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose biphosphate carboxylase oligomers in Escherichia coli. Nature 337: 44-47.
25. Goloubinoff P, Christeller JT, Gatenby AA, Lorimer GH, (1989) Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP. Nature 342: 884-889.
26. Grallert H, Rutkat K, Buchner J, (1998) GroEL traps dimeric and monomeric unfolding intermediates of citrate synthase. J Biol Chem 273: 33305-33310.
27. Walsh JL, Keuth TJ, Knull HR, (1989) Glycolytic enzyme interactions with tubulin and microtubules. Biochim Biophys Acta 999: 64-70.
28. Knull HR, Walsh JL, (1992) Association of glycolytic enzymes with cytoskeleton. Curr Top Cell Regul 33: 15-30.
29. Orosz F, Olah H, Alvárez M, Keseru GM, Szabo B, et al.(2001) Distinct behavior of mutant triosephosphate isomerase in hemolysate and in isolated form: molecular basis of enzyme deficiency. Blood 98: 3106-3112.
30. Orosz F, Wágner G, Liliom K, Kovács J, Baróti K, et al.(2000) Enhanced association of mutant triosephosphate isomerase to red cell membranes and to brain microtubules. Proc Natl Acad Sci U S A 97: 1026-1031.
31. Dhar-Chowdhury P, Harell MD, Han SY, Jakowska D, Parachuru L, et al.(2005) The glycolytic enzymes, glyceraldehydes-3-phosphate dehydrogenase, triose-phosphate isomerase, and pyruvate kinase are components of the KATP channel macromolecular complex and regulate its function. J Biol Chem 280: 38464-38470.
32. Walden H, Taylor G, Lilie H, Knura T, Hensel R, (2004) Triosephosphate isomerase of the hyperthermophile Thermoproteius tenax: thermostability is not everything. Biochem Soc Trans 32: 305.
33. Walden H, Taylor GL, Lorentzen E, Pohl E, Lilie H, et al.(2004) Structure and function of a regulated archaeal triosephosphate isomerase adapted to high temperture. J Mol Biol 342: 861-875.
34. Srere PA, (2000) Macromolecular interactions: tracing the roots. Trends in Biochem Sci 25: 150-153.
35. Srere PA, Ovadi J, (1990) Enzyme-enzyme interactions and their metabolic role. FEBS Lett 268: 360-364.
36. Rakus D, Pasek M, Krotkiewski H, Dzugaj A, (2004) Interaction between muscle aldolase and muscle fructose 1,6-biphosphatase results in the substrate channeling. Biochemistry 43: 14948-14957.
37. Borchet TV, Pratt K, Zeelen JP, Callens M, Noble ME, et al.(1993) Overexpression of trypanosomal triosephosphate isomerase in Escherichia coli and caracterisation of a dimer-interface mutant. Eur J Biochem 211: 703-710.
38. Ostoa-Saloma P, Garza-Ramos G, Ramírez J, Becker I, Berzunza M, et al.(1997) Cloning, expression, purification and characterization of triosephosphate isomerase from Trypanosoma cruzi. Eur J Biochem 244: 700-705.
39. Kohl L, Callens M, Wierenga RK, Opperdoes FR, Micels PA, (1994) Triose-phosphate isomerase of Leishmania mexicana mexicana. Cloning and characterization of the gene, overexpression in Escherichia coli and analysis of the protein. Eur J Biochem 220: 331-338.
40. Vázquez-Contreras E, Zubillaga RA, Mendoza-Hernández G, Costas M, Fernández-Velasco DA, (2000) Equilibrium unfolding of yeast triosephosphate isomerase: a monomeric intermediate in guanidine-HCl and two-state behavior in urea. Protein Pept. Letters 7: 57-64.
41. Pace NC, Vajdos F, Fee L, Grimsley G, Gray T, (1995) How to measure and predict the molar absorption coefficient of a protein. Protein Sci 4: 2411-2423.
42. Maruyama T, Katoh S, Nakajima M, Nabetani H, (2001) Mechanism of bovine serum albumin aggregation during ultrafiltration. Biotech Bioeng 75: 233-238.
43. Bulone D, Vincenzo M, San Biagio PL, (2001) Effects of intermediates on aggregation of native bovine serum albumin. Biophysical Chemistry 91: 61-69.
44. Banerjeee SK, Pogolotti A Jr, Rupley JA, (1975) Self-association of lysozyme. J Biol Chem 250: 8260-8266.
45. Hampe OG, Tondo CV, Hasson-Voloch A, (1982) A biophysical model of lysozyme self-association. Biophys J 39: 77-82.