Secondary-structure characterization by far-UV CD of highly purified uncoupling protein 1 expressed in yeast

Biochemical Journal

Volumn 380, Issue 1, 2004, Pages 139-145

  Douette, Pierre ^a   Navet, Rachel ^a   Bouillenne, Fabrice ^a   Brans, Alain ^a   Sluse Goffart, Claudine ^a   Matagne, André ^a   Sluse, Francis E ^a  

^a UNIVERSITY OF LIÈGE   (Belgium)

Author keywords

CD; Fluorescence resonance energy transfer; Homology modelling; Mitochondrial membrane protein; Secondary structure; Uncoupling protein

Indexed keywords

BIOLOGICAL MEMBRANES; ENERGY DISSIPATION; ENERGY TRANSFER; FLUORESCENCE; PROTEINS; PURIFICATION; RESONANCE; ULTRAVIOLET RADIATION; YEAST;

BINDING CAPACITY; BINDING MECHANISM;

BIOCHEMISTRY;

ADENINE NUCLEOTIDE TRANSLOCASE; EPITOPE; PURINE NUCLEOTIDE; UNCOUPLING PROTEIN 1;

ALPHA HELIX; AMINO ACID SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; FLUORESCENCE RESONANCE ENERGY TRANSFER; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN PURIFICATION; PROTEIN STRUCTURE; RAT; SACCHAROMYCES CEREVISIAE; ULTRAVIOLET RADIATION; YEAST;

AMINO ACID SEQUENCE; ANIMALS; CARRIER PROTEINS; CATTLE; CHROMATOGRAPHY, AFFINITY; CIRCULAR DICHROISM; FLUORESCENCE RESONANCE ENERGY TRANSFER; ION CHANNELS; MEMBRANE PROTEINS; MITOCHONDRIA; MITOCHONDRIA, HEART; MITOCHONDRIAL ADP, ATP TRANSLOCASES; MITOCHONDRIAL PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, SECONDARY; RATS; RECOMBINANT FUSION PROTEINS; SACCHAROMYCES CEREVISIAE; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID;

SACCHAROMYCES; SACCHAROMYCES CEREVISIAE;

EID: 2642574988     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20031957     Document Type: Article

References (39)

1. Walker, J. E. (1992) The mitochondrial transporter family. Curr. Opin. Struct. Biol. 2, 519-526
2. Klingenberg, M. and Echtay, K. S. (2001) Uncoupling proteins: the issues from a biochemist point of view. Biochim. Biophys. Acta 1504, 128-143
3. Echtay, K. S., Winkler, E. and Klingenberg, M. (2000) Coenzyme Q is an obligatory cofactor for uncoupling protein function. Nature (London) 408, 609-613
4. Runswick, M. J., Powell, S. J., Nyren, P. and Walker, J. E. (1987) Sequence of the bovine mitochondrial phosphate carrier protein: structural relationship to ADP/ATP translocase and the brown fat mitochondria uncoupling protein. EMBO J. 6, 1367-1373
5. Walker, J. E. and Runswick, M. J. (1993) The mitochondrial transport protein superfamily. J. Bioenerg. Biomembr. 25, 435-446
6. Miroux, B., Frossard, V., Raimbault, S., Ricquier, D. and Bouillaud, F. (1993) The topology of the brown adipose tissue mitochondrial uncoupling protein determined with antibodies against its antigenic sites revealed by a library of fusion proteins. EMBO J. 12, 3739-3745
7. El Moualij, B., Duyckaerts, C., Lamotte-Brasseur, J. and Sluse, F. E. (1997) Phylogenetic classification of the mitochondrial carrier family of Saccharomyces cerevisiae. Yeast 13, 573-581
8. Klingenberg, M. (1990) Mechanism and evolution of the uncoupling protein of brown adipose tissue. Trends Biochem. Sci. 15, 108-112
9. Pebay-Peyroula, E., Dahout-Gonzalez, C., Kahn, R., Trezeguet, V., Lauquin, G. J. and Brandolin, G. (2003) Structure of mitochondrial ADP/ATP carrier in complex with carboxyatractyloside. Nature (London) 426, 39-44
10. Murdza-Inglis, D. L., Patel, H. V., Freeman, K. B., Jezek, P., Orosz, D. E. and Garlid, K. D. (1991) Functional reconstitution of rat uncoupling protein following its high level expression in yeast. J. Biol. Chem. 266, 11871-11875
11. Bathgate, B., Freebairn, E. M., Greenland, A. J. and Reid, G. A. (1992) Functional expression of the rat brown adipose tissue uncoupling protein in Saccharomyces cerevisiae. Mol. Microbiol. 6, 363-370
12. Stuart, J. A., Harper, J. A., Brindle, K. M., Jekabsons, M. B. and Brand, M. D. (2001) A mitochondrial uncoupling artifact can be caused by expression of uncoupling protein 1 in yeast. Biochem. J. 356, 779-789
13. Kozak, M. (1986) Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes. Cell (Cambridge, Mass.) 44, 283-292
14. Daum, G., Bohni, P. C. and Schatz, G. (1982) Import of proteins into mitochondria. Cytochrome b2 and cytochrome c peroxidase are located in the intermembrane space of yeast mitochondria. J. Biol. Chem. 257, 13028-13033
15. Lobley, A. and Wallace, B. A. (2001) DICHROWEB: a website for the analysis of protein secondary structure from circular dichroism spectra. Biophys. J. 80, 373a
16. Lobley, A., Whitmore, L. and Wallace, B. A. (2002) DICHROWEB: an interactive website for the analysis of protein secondary structure from circular dichroism spectra. Bioinformatics 18, 211-212
17. Compton, L. A. and Johnson, Jr, W. C. (1986) Analysis of protein circular dichroism spectra for secondary structure using a simple matrix multiplication. Anal. Biochem. 155, 155-167
18. Manavalan, P. and Johnson, Jr, W. C. (1986) Variable selection method improves the prediction of protein secondary structure from circular dichroism spectra. Anal. Biochem. 167, 76-85
19. Sreerema, N. and Woody, R. W. (1993) A self-consistent method for the analysis of protein secondary structure from circular dichroism. Anal. Biochem. 209, 32-44
20. Sreerema, N., Venyaminov, S. Y. and Woody, R. W. (1999) Estimation of the number of helical and strand segments in proteins using CD spectroscopy. Protein Sci. 8, 370-380
21. Sreerama, N. and Woody, R. W. (2000) Estimation of protein secondary structure from CD spectra: comparison of CONTIN, SELCON and CDSSTR methods with an expanded reference set. Anal. Biochem. 287, 252-260
22. Guex, N. and Peitsch, M. C. (1997) SWISS-MODEL and the Swiss-Pdb Viewer: an environment for comparative protein modelling. Electrophoresis 18, 2714-2723
23. Laskowski, R. A., MacArthur, M. W., Moss, D. S. and Thornton, J. M. (1993) PROCHECK - a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291
24. Lin, C. S. and Klingenberg, M. (1980) Isolation of the uncoupling protein from brown adipose tissue mitochondria. FEBS Lett. 113, 299-303
25. Lin, C. S. and Klingenberg, M. (1982) Characteristics of the isolated purine nucleotide binding protein from brown fat mitochondria. Biochemistry 21, 2950-2956
26. Fiore, C., Trezeguet, V., Roux, P., Le Saux, A., Noel, F., Schwimmer, C., Arlot, D., Dianoux, A. C., Lauquin, G. J. and Brandolin, G. (2000) Purification of histidine-tagged mitochondrial ADP/ATP carrier: influence of the conformational states of the C-terminal region. Protein Expr. Purif. 19, 57-65
27. Huang, S. G. and Klingenberg, M. (1995) Fluorescent nucleotide derivatives as specific probes for the uncoupling protein: thermodynamics and kinetics of binding and the control by pH. Biochemistry 34, 349-360
28. Jekabsons, M. B., Echtay, K. S. and Brand, M. D. (2002) Nucleotide binding to human uncoupling protein-2 refolded from bacterial inclusion bodies. Biochem. J. 366, 565-571
29. Johnson, Jr, W. C. (1990) Protein secondary structure and circular dichroism: a practical guide. Proteins 7, 205-214
30. Wallace, B. A., Lees, J. G., Orry, A. J., Lobley, A. and Janes, R. W. (2003) Analyses of circular dichroism spectra of membrane proteins. Protein Sci. 12, 875-884
31. Wallace, B. A. and Mao, D. (1984) Circular dichroism analyses of membrane proteins: an examination of differential light scattering and absorption flattening effects in large membrane vesicles and membrane sheets. Anal. Biochem. 142, 317-328
32. Wallace, B. A. and Teeters, C. L. (1987) Differential absorption flattening optical effects are significant in the circular dichroism spectra of large membrane fragments. Biochemistry 26, 65-70
33. Kaback, H. R., Frillingos, S., Jung, H., Jung, K., Prive, G. G., Ujwal, M. L., Weitzman, C., Wu, J. and Zen, K. (1994) The lactose permease meets Frankenstein. J. Exp. Biol. 196, 183-195
34. Abramson, J., Smirnova, I., Kasho, V., Verner, G., Kaback, H. R. and Iwata, S. (2003) Structure and mechanism of the lactose permease of Escherichia coli. Science 301, 610-615
35. Mielke, D. L. and Wallace, B. A. (1988) Secondary structural analyses of the nicotinic acetylcholine receptor as a test of molecular models. J. Biol. Chem. 263, 3177-3182
36. Brejc, K., van Dijk, W. J., Klaassen, R. V., Schuurmans, M., van der Oost, J., Smit, A. B. and Sixma, T. K. (2001) Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors. Nature (London) 411, 269-276
37. Miyazawa, A., Fujiyoshi, Y. and Unwin, N. (2003) Structure and gating mechanism of the acetylcholine receptor pore. Nature (London) 423, 949-955
38. +-ATPase proteolipid in phospholipid vesicles. Biochemistry 21, 4960-4968
39. Nelson, D. R., Felix, C. M. and Swanson, J. M. (1998) Highly conserved charge-pair network in the mitochondrial carrier family. J. Mol. Biol. 277, 285-308