A 2D-IR study of heat- and [13C]urea-induced denaturation of sarcoplasmic reticulum Ca2+-ATPase.

• Authors: Ibón Iloro , Félix M Goñi , José L R Arrondo
• Languages of publication: EN

Abstracts

EN

Two-dimensional infrared correlation spectroscopy (2D-IR) was applied to the study of urea- and heat-induced unfolding denaturation of sarcoplasmic reticulum Ca^(2+)-ATPase (SR ATPase). Urea at 2-3 M causes reversible loss of SR ATPase activity, while higher concentrations induce irreversible denaturation. Heat-induced denaturation is a non-two-state process, with an "intermediate state" (at t ≈ 45°C) characterized by the presence of protein monomers, instead of the native oligomers. 2D-IR reveals that urea denaturation causes loss of the structural transition to the "intermediate state". Whenever the urea effect can be reversed, the transition to the "intermediate state" is re-established.

Keywords

EN

2D-IR; urea-induced denaturation; sarcoplasmic reticulum; heat-induced denaturation

• Journal: Acta Biochimica Polonica
• Year: 2005
• Volume: 52
• Issue: 2
• Pages: 477-483

Dates

published

2005

received

2005-05-10

accepted

2005-05-13

revised

2005-05-13

Contributors

author

Ibón Iloro

• Unidad de Biofísica (Centro Mixto CSIC-UPV/EHU), and Departamento de Bioquímica, Universidad del País Vasco, Bilbao, Spain

author

Félix M Goñi

• Unidad de Biofísica (Centro Mixto CSIC-UPV/EHU), and Departamento de Bioquímica, Universidad del País Vasco, Bilbao, Spain

author

José L R Arrondo

• Unidad de Biofísica (Centro Mixto CSIC-UPV/EHU), and Departamento de Bioquímica, Universidad del País Vasco, Bilbao, Spain

References

• Arrondo JL, Urbaneja MA, Goni FM, Macarulla JM, Sarzala G (1985) Protein conformational transitions in sarcoplasmic reticulum membranes. Biochem Biophys Res Commun 128: 1159-1163.
• Arrondo JL, Mantsch HH, Mullner N, Pikula S, Martonosi A (1987) Infrared spectroscopic characterization of the structural changes connected with the E1----E2 transition in the Ca2+-ATPase of sarcoplasmic reticulum. J Biol Chem 262: 9037-9043.
• Arrondo JL, Muga A, Castresana J, Goni FM (1993) Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy. Prog Biophys Mol Biol 59: 23-56.
• Arrondo JL, Castresana J, Valpuesta JM, Goni FM (1994) Structure and thermal denaturation of crystalline and noncrystalline cytochrome oxidase as studied by infrared spectroscopy. Biochemistry 33: 11650-11655.
• Arrondo JL, Goñi FM (1999) Structure and dynamics of membrane proteins as studied by infrared spectroscopy. Prog Biophys Mol Biol 72: 367-405.
• Arrondo JL, Echabe I, Iloro I, Hernando MA, de la Cruz F, Goni FM (2003) A bacterial TrwC relaxase domain contains a thermally stable alpha-helical core. J Bacteriol 185: 4226-4236.
• Bañuelos S, Arrondo JL, Goni FM, Pifat G (1995) Surface-core relationships in human low density lipoprotein as studied by infrared spectroscopy. J Biol Chem 270: 9192-9196.
• Barth A, Kreutz W, Mantele W (1994) Changes of protein structure, nucleotide microenvironment, and Ca(2+)-binding states in the catalytic cycle of sarcoplasmic reticulum Ca(2+)-ATPase: investigation of nucleotide binding, phosphorylation and phosphoenzyme conversion by FTIR difference spectroscopy. Biochim Biophys Acta 1194: 75-91.
• Barth A, von Germar F, Kreutz W, Mantele W (1996) Time-resolved infrared spectroscopy of the Ca2+-ATPase. The enzyme at work. J Biol Chem 271: 30637-30646.
• Buchet R, Jona I, Martonosi A (1989) Correlation of structure and function in the Ca2+-ATPase of sarcoplasmic reticulum: a Fourier transform infrared spectroscopy (FTIR) study on the effects of dimethyl sulfoxide and urea. Biochim Biophys Acta 983: 167-178.
• Contreras LM, Aranda FJ, Gavilanes F, Gonzalez-Ros JM, Villalain J (2001) Structure and interaction with membrane model systems of a peptide derived from the major epitope region of HIV protein gp41: implications on viral fusion mechanism. Biochemistry 40: 3196-3207.
• Daniel RM, Dines M, Petach HH (1996) The denaturation and degradation of stable enzymes at high temperatures. Biochem J 317: 1-11.
• Echabe I, Dornberger U, Prado A, Goni FM, Arrondo JL (1998) Topology of sarcoplasmic reticulum Ca2+-ATPase: an infrared study of thermal denaturation and limited proteolysis. Protein Sci 7: 1172-1179.
• Fabian H, Mantsch HH, Schultz CP (1999) Two-dimensional IR correlation spectroscopy: sequential events in the unfolding process of the lambda cro-V55C repressor protein. Proc Natl Acad Sci USA 96: 13153-13158.
• Glabe CG (2004) Conformation-dependent antibodies target diseases of protein misfolding. Trends Biochem Sci 29: 542-547.
• Iloro I, Chehin R, Goni FM, Pajares MA, Arrondo JL (2004) Methionine adenosyltransferase alpha-helix structure unfolds at lower temperatures than beta-sheet: a 2D-IR study. Biophys J 86: 3951-3958.
• Inesi G, Millman M, Eletr S (1973) Temperature-induced transitions of function and structure in sarcoplasmic reticulum membranes. J Mol Biol 81: 483-504.
• Kumar TK, Yu C (2004) Monitoring protein folding at atomic resolution. Acc Chem Res 37: 929-936.
• Lepock JR (2005) Measurement of protein stability and protein denaturation in cells using differential scanning calorimetry. Methods 35: 117-125.
• Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the Folin phenol reagent. J Biol Chem 193: 265-275.
• Martonosi AN (1996) Structure-function relationships in the Ca(2+)-ATPase of sarcoplasmic reticulum: facts, speculations and questions for the future. Biochim Biophys Acta 1275: 111-117.
• Martonosi AN, Pikula S (2003) The structure of the Ca2+-ATPase of sarcoplasmic reticulum. Acta Biochim Polon 50: 337-365.
• Mayne L, Englander SW (2000) Two-state vs. multistate protein unfolding studied by optical melting and hydrogen exchange. Protein Sci 9: 1873-1877.
• Meissner G (1974) Isolation of sarcoplasmic reticulum from skeletal muscle. Methods Enzymol 31: 238-246.
• Nakamura H, Jilka RL, Boland R, Martonosi AN (1976) Mechanism of ATP hydrolysis by sarcoplasmic reticulum and the role of phospholipids. J Biol Chem. 251: 5414-5423.
• Paquet MJ, Laviolette M, Pezolet M, Auger M (2001) Two-dimensional infrared correlation spectroscopy study of the aggregation of cytochrome c in the presence of dimyristoylphosphatidylglycerol. Biophys J 81: 305-312.
• Pastrana-Rios B, Ocana W, Rios M, Vargas GL, Ysa G, Poynter G, Tapia J, Salisbury JL (2002) Centrin: its secondary structure in the presence and absence of cations. Biochemistry 41: 6911-6919.
• Prado A, Arrondo JL, Villena A, Goni FM, Macarulla JM (1983) Membrane-surfactant interactions. The effect of Triton X-100 on sarcoplasmic reticulum vesicles. Biochim Biophys Acta 733: 163-171.
• Reinstädler D, Fabian H, Backmann J, Naumann D (1996) Refolding of thermally and urea-denatured ribonuclease A monitored by time-resolved FTIR spectroscopy. Biochemistry 35: 15822-15830.
• Shanmukh S, Howell P, Baatz JE, Dluhy RA (2002) Effect of hydrophobic surfactant proteins SP-B and SP-C on phospholipid monolayers. Protein structure studied using 2D IR and beta correlation analysis. Biophys J 83: 2126-2141.
• Soloaga A, Ramirez JM, Goni FM (1998) Reversible denaturation, self-aggregation, and membrane activity of Escherichia coli alpha-hemolysin, a protein stable in 6 M urea. Biochemistry 37: 6387-6393.
• Tanford C (1968) Protein denaturation. Adv Protein Chem 23: 121-282.
• Torrecillas A, Corbalan-Garcia S, Gomez-Fernandez JC (2003) Structural study of the C2 domains of the classical PKC isoenzymes using infrared spectroscopy and two-dimensional infrared correlation spectroscopy. Biochemistry 42: 11669-11681.
• Toyoshima C, Nakasako M, Nomura H, Ogawa H (2000) Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution. Nature 405: 647-655.
• Turnay J, Olmo N, Gasset M, Iloro I, Arrondo JL, Lizarbe MA (2002) Calcium-dependent conformational rearrangements and protein stability in chicken annexin A5. Biophys J 83: 2280-2291.
• Villalain J, Gomez-Fernandez JC, Jackson M, Chapman D (1989) Fourier transform infrared spectroscopic studies on the secondary structure of the Ca2+-ATPase of sarcoplasmic reticulum. Biochim Biophys Acta 978: 305-312.
• Waldner JC, Lahr SJ, Edgell MH, Pielak GJ (1999) Nonideality and protein thermal denaturation. Biopolymers 49: 471-479.