Topology of sarcoplasmic reticulum Ca2+-ATPase: An infrared study of thermal denaturation and limited proteolysis

Protein Science

Volumn 7, Issue 5, 1998, Pages 1172-1179

  Echabe, Izaskun ^a   Dornberger, Utz ^b   Prado, Adelina ^a   Goñi, Félix M ^a   Arrondo, José Luis R ^a  

^a UNIVERSITY OF THE BASQUE COUNTRY UPV EHU   (Spain)

^b FRIEDRICH SCHILLER UNIVERSITY JENA   (Germany)

Author keywords

Ca2+ ATPase; Infrared spectroscopy; Protein structure; Proteolysis; Sarcoplasmic reticulum; Thermal analysis

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); BUFFER; DEUTERIUM OXIDE; MONOMER; OLIGOMER; WATER;

ALPHA HELIX; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME DENATURATION; ENZYME LOCALIZATION; INFRARED SPECTROSCOPY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN SECONDARY STRUCTURE; RABBIT; SARCOPLASMIC RETICULUM;

ANIMALIA; ORYCTOLAGUS CUNICULUS;

EID: 0031807972     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560070511     Document Type: Article

References (46)

1. 2+ pump mechanism. Biochim Biophys Acta 988:47-12.
2. Arrondo JLR, Blanco FJ, Serrano L, Goñi FM. 1996. Infrared evidence of a β-hairpin peptide structure in solution. FEBS Lett 384:35-51.
3. Arrondo JLR, Castresana J, Valpuesta JM, Goñi FM. 1994. The structure and thermal denaturation of crystalline and non-crystalline cytochrome oxidase as studied by infrared spectroscopy. Biochemistry 33:11650-11655.
4. Arrondo JLR, Goñi FM. 1993. Infrared spectroscopic studies of lipid-protein interactions in membranes. In: Watts A, eds. Protein-lipid interactions. Amsterdam: Elsevier Science Publishers. pp 321-349.
5. 2+-ATPase of sarcoplasmic reticulum. J Biol Chem 262:9037-9043.
6. Arrondo JLR, Muga A, Castresana J, Bernabeu C, Gõni FM. 1989. An infrared spectroscopic study of β-galactosidase structure in aqueous solutions. FEBS Lett 252:118-120.
7. Arrondo JLR, Muga A, Castresana J, Goñi FM. 1993. Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy. Prog Biophys Mol Biol 59:23-56.
8. Banuelos S, Arrondo JLR, Goñi FM, Pifat G. 1995. Surface-core relationships in human low density lipoprotein as studied by infrared spectroscopy. J Biol Chem 270:9192-9196.
9. 2+-ATPase: Investigation of nucleotide binding, phosphorylation and phosphoenzyme conversion by FTIR difference spectroscopy. Biochim Biophys Acta 1194:75-91.
10. 2+-ATPase - The enzyme at work. J Biol Chem 271:30637-30646.
11. 2+ alters the FTIR spectrum of sarcoplasmic reticulum. Biochim Biophys Acta 1069:209-217.
12. Byler DM, Susi H. 1986. Examination of the secondary structure of proteins by deconvolved FTIR spectra. Biopolymers 25:469-487.
13. Casal HL, Cameron DG, Smith ICP, Mantsch HH. 1980. Acholeplasma laid-lawii membranes: A Fourier transform infrared study of the influence of protein on lipid organization and dynamics. Biochemistry 19:444-451.
14. Castresana J, Muga A, Arrondo JLR. 1988. The structure of proteins in aqueous solutions. An assessment of triose phosphate isomerase structure by Fourier-transform infrared spectroscopy. Biochem Biophys Res Commun 152:69-75.
15. Cohen C, Parry DA. 1986. α-Helical coiled coils - A widespread motif in proteins. Trends Biochem Sci 11:245-248.
16. 2+)-ATPase from sarcoplasmic reticulum leads to a highly hydrophobic proteinaceous residue with a mainly α-helical structure. Biochemistry 33:8247-8254.
17. 2+-ATPase in biomembranes and reconstituted systems. J Mol Biol 157:597-618.
18. De Jongh HHJ, Goormaghtigh E, Ruysschaert JM. 1996. The different molar absorptivities of the secondary structure types in the amide I region: An attenuated total reflection infrared study on globular proteins. Anal Biochem 242:95-103.
19. Earnest TN, Herzfeld J, Rothschild KJ. 1990. Polarized Fourier transform infrared spectroscopy of bacteriorhodopsin. Transmembrane alpha helices are resistant to hydrogen/deuterium exchange. Biophys J 58:1539-1546.
20. Echabe I, Arrondo JLR. 1995. Infrared studies of eukaryotic and prokaryotic cytochrome c oxidases. In: Merlin JC, Turrell S, Huvenne JP, eds. Spectroscopv of biological molecules. Dordrecht: Kluwer Academic Publishers. pp 123-126.
21. Echabe I, Haltia T, Freire E, Goñi FM, Arrondo JLR. 1995. Subunit III of cytochrome c oxidase influences the conformation of subunits I and II: An infrared study. Biochemistry 34:13565-13569.
22. Fabian H, Naumann D, Misselwitz R, Ristau O, Gerlach D, Welfle H. 1992. Secondary structure of streptokinase in aqueous solution: A Fourier transform infrared spectroscopic study. Biochemistry 31:6532-6538.
23. +-ATPase monitored by hydrogen/deuterium exchange kinetics. A Fourier transform infrared spectroscopy approach. J Biol Chem 269:27409-27413.
24. Görne-Tschelnokow U, Strecker A, Kaduk C, Naumann D, Hucho F. 1994. The transmembrane domains of the nicotinic acetylcholine receptor contain α-helical and β-structures. EMBO J 13:338-341.
25. Haltia T, Semo N, Arrondo JLR, Goñi FM, Freire E. 1994. Thermodynamic and structural stability of cytochrome c oxidase from Paracoccus dentrificans. Biochemists 33:9731-9740.
26. 5 in solution by Fourier-transform infrared spectroscopy. Biochemistry 28:931-935.
27. Inesi G. Millman M, Eletr S. 1973. Temperature-induced transitions of function and structure in sarcoplasmic reticulum membranes. J Mol Biol 81:483-504.
28. 2+-ATPase retain their functional Ca binding properties after removal of cytoplasmic fragments by proteinase K? J Biol Chem 270:20123-20134.
29. 4. Nature 193:680-685.
30. Lepock JR, Rodahl AM, Zhang C, Heynen ML, Waters B, Cheng KH. 1990. Thermal denaturation of the Ca2(+)-ATPase of sarcoplasmic reticulum reveals two thermodynamically independent domains. Biochemistry 29(3):681-689.
31. Lowry OH, Rosebrough N, Fair AL, Randall RJ. 1951. Protein measurement with the Folin phenol reagent. J Biol Chem 193:265-275.
32. 2+-dependent ATPase from rabbit muscle deduced from its complementary DNA sequence. Nature 316:696-100.
33. Martínez A, Haavik J, Flatmark T, Arrondo JLR, Muga A. 1996. Conformational properties and stability of tyrosine hydroxylase studied by infrared spectroscopy - Effect of iron/catecholamine binding and phosphorylation. J Biol Chem 271:19737-19742.
34. 2+-ATPase of sarcoplasmic reticulum: Facts, speculations and questions for the future. Biochim Biophys Acta 1275:111-117.
35. ++ binding proteins. Biochim Biophys Acta 295:246-269.
36. Merino JM, Moller JV, Gutiérrez-Merino C. 1994. Thermal unfolding of monomeric Ca(II), Mg(II)-ATPase from sarcoplasmic reticulum of rabbit skeletal muscle. FEBS Lett 3:155-159.
37. 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.
38. Prado A, Arrondo JLR, Villena A, Goñi FM, Macarulla JM. 1983. Membrane-surfactant interactions. The effect of Triton X-100 on sarcoplasmic reticulum vesicles. Biochim Biophys Acta 733:163-171.
39. Reisdorf WC Jr, Krimm S. 1996. Infrared amide I′ band of the coiled coil. Biochemistry 35:1383-1386.
40. Stewart PS, MacLennan DH, Shamoo AE. 1976. J Biol Chem 257:712-719.
41. Stokes DL, Taylor WR, Green NM. 1994. .Structure, transmembrane topology and helix packing of P-type ion pumps. FEBS Lett 346:32-38.
42. Susi H. 1969. Infrared spectra of biological macromolecules and related systems. In: Timasheff SN, Stevens L, eds. Structure and stability of biological macromolecules. New York: Dekker. pp 575-663.
43. Toyoshima C, Sarabe H, Stokes DL. 1993. Three-dimensional cryo-electron microscopy of the calcium ion pump in the sarcoplasmic reticulum membrane. Nature 362:469-471.
44. +-ATPase and of its membrane-associated proteolytic peptides. J Biol Chem 270:17685-17696.
45. Villalaín J, Gómez-Fernández JC, Jackson M, Chapman D. 1989. FT-IR spectroscopic studies on the secondary structure of the CA++-ATPase of sarcoplasmic reticulum. Biochim Biophys Acta 1050:29-33.
46. Yang PW, Manisch HH, Arrondo JLR, Saint-Girons I, Guillou Y, Cohen GN, Barzu O. 1987. Fourier transform infrared investigation of the Escherichia coli methionine aporepressor. Biochemistry 26:2706-2711.