Urea unfolding of opsin in phospholipid bicelles

Photochemistry and Photobiology

Volumn 85, Issue 2, 2009, Pages 494-500

  McKibbin, Craig ^a,c   Farmer, Nicola A ^a   Edwards, Patricia C ^b   Villa, Claudio ^b   Booth, Paula J ^a  

^a UNIVERSITY OF BRISTOL   (United Kingdom)

^b MRC LABORATORY OF MOLECULAR BIOLOGY   (United Kingdom)

^c UNIVERSITY OF MANCHESTER   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

1,2 DIHEXADECYL SN GLYCERO 3 PHOSPHOCHOLINE; 1,2-DIHEXADECYL-SN-GLYCERO-3-PHOSPHOCHOLINE; 3 ((3 CHOLAMIDOPROPYL)DIMETHYLAMMONIUM) 1 PROPANESULFONATE; 3-((3-CHOLAMIDOPROPYL)DIMETHYLAMMONIUM)-1-PROPANESULFONATE; CHOLIC ACID DERIVATIVE; DIMYRISTOYLPHOSPHATIDYLCHOLINE; ETHER PHOSPHOLIPID; OPSIN; PHOSPHOLIPID; TRYPTOPHAN; UREA;

ANIMAL; CATTLE; CHEMISTRY; CONFERENCE PAPER; KINETICS; METABOLISM; PROTEIN FOLDING; SPECTROPHOTOMETRY;

ANIMALS; CATTLE; CHOLIC ACIDS; DIMYRISTOYLPHOSPHATIDYLCHOLINE; KINETICS; OPSINS; PHOSPHOLIPID ETHERS; PHOSPHOLIPIDS; PROTEIN FOLDING; SPECTROPHOTOMETRY; TRYPTOPHAN; UREA;

BOVINAE;

EID: 60849096672     PISSN: 00318655     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1751-1097.2008.00503.x     Document Type: Conference Paper

References (37)

1. Mayor, U., N. Guydosh, C. Johnson, J. Grossmann, S. Sato, G. Jas, S. Freund, D. Alonso, V. Daggett A. Fersht (2003) The complete folding of a protein from nanoseconds to microseconds. Nature 421, 863 867.
2. London, E. H. G. Khorana (1982) Denaturation and renaturation of bacteriorhodopsin in detergents and lipid-detergent mixtures. J. Biol. Chem. 257, 7003 7011.
3. Booth, P. J. P. Curnow (2006) Membrane proteins shape up: Understanding in vitro folding. Curr. Opin. Struct. Biol. 16, 480 488.
4. Lagerstrom, M. H. Schioth (2008) Structural diversity of G protein-coupled receptors and significance for drug discovery. Nat. Rev. Drug Discov. 7, 339 357.
5. Vold, R. R., R. S. Prosser A. J. Deese (1997) Isotropic solutions of phospholipid bicelles: A new membrane mimetic for high-resolution NMR studies of polypeptides. J. Biomol. NMR 9, 329 335.
6. Baneres, J. L., D. Mesnier, A. Martin, L. Joubert, A. Dumuis J. Bockaert (2005) Molecular characterization of a purified 5-HT4 receptor: A structural basis for drug efficacy. J. Biol. Chem. 280, 20253 20260.
7. Rasmussen, S., H. Choi, D. Rosenbaum, T. Kobilka, F. Thian, P. Edwards, M. Burghammer, V. Ratnala, R. Sanishvili, R. Fischetti, G. Schertler, W. Weis B. Kobilka (2007) Crystal structure of the human beta2 adrenergic G protein-coupled receptor. Nature 450, 383 387.
8. Okada, T., O. P. Ernst, K. Palczewski K. P. Hofmann (2001) Activation of rhodopsin: New insights from structural and biochemical studies. Trends Biochem. Sci. 26, 318 324.
9. Okada, T., K. Takeda T. Kouyama (1998) Highly selective separation of rhodopsin from bovine rod outer segment membranes using combination of divalent cation and alkyl(thio)glucoside. Photochem. Photobiol. 67, 495 499.
10. Park, J. H., P. Scheerer, K. P. Hofmann, H. W. Choe O. P. Ernst (2008) Crystal structure of the ligand-free G-protein-coupled receptor opsin. Nature 454, 183 187.
11. Stubbs, G. W. B. J. Litman (1978) Effect of alterations in the amphipathic microenvironment on the conformational stability of bovine opsin. 2. Rate of loss of opsin regenerability. Biochemistry 17, 220 225.
12. De Grip, W. J. (1982) Thermal stability of rhodopsin and opsin in some novel detergents. Methods Enzymol. 81, 256 265.
13. Sakamoto, T. H. G. Khorana (1995) Structure and function in rhodopsin: The fate of opsin formed upon the decay of light-activated metarhodopsin II in vitro. Proc. Natl Acad. Sci. USA 92, 249 253.
14. McKibbin, C., A. Toye, P. Reeves, H. Khorana, P. Edwards, C. Villa P. Booth (2007) Opsin stability and folding: The role of Cys185 and abnormal disulfide bond formation in the intradiscal domain. J. Mol. Biol. 374, 1309 1318.
15. Reeves, P. J., J. Hwa H. G. Khorana (1999) Structure and function in rhodopsin: Kinetic studies of retinal binding to purified opsin mutants in defined phospholipid-detergent mixtures serve as probes of the retinal binding pocket. Proc. Natl Acad. Sci. USA 96, 1927 1931.
16. McKibbin, C., N. Farmer, C. Jeans, P. Reeves, H. Khorana, B. Wallace, P. Edwards, C. Villa P. Booth (2007) Opsin stability and folding: Modulation by phospholipid bicelles. J. Mol. Biol. 374, 1319 1332.
17. Edwards, P. C., J. Li, M. Burghammer, J. H. McDowell, C. Villa, P. A. Hargrave G. F. Schertler (2004) Crystals of native and modified bovine rhodopsins and their heavy atom derivatives. J. Mol. Biol. 343, 1439 1450.
18. Wald, G. P. K. Brown (1953) The molar extinction of rhodopsin. J. Gen. Physiol. 37, 189 200.
19. Wald, G. P. K. Brown (1956) Synthesis and bleaching of rhodopsin. Nature 177, 174 176.
20. Farrens, D. L. H. G. Khorana (1995) Structure and function in rhodopsin. Measurement of the rate of metarhodopsin II decay by fluorescence spectroscopy. J. Biol. Chem. 270, 5073 5076.
21. McKibbin, C., N. A. Farmer, C. Jeans, P. J. Reeves, H. G. Khorana, B. A. Wallace, P. C. Edwards, C. Villa P. J. Booth (2007) Opsin stability and folding: Modulation by phospholipid bicelles. J. Mol. Biol. 374, 1319 1332.
22. Radding, C. M. G. Wald (1956) The stability of rhodopsin and opsin; effects of pH and aging. J. Gen. Physiol. 39, 923 933.
23. Hubbard, R. (1958) The thermal stability of rhodopsin and opsin. J. Gen. Physiol. 42, 259 280.
24. Landin, J. S., M. Katragadda A. D. Albert (2001) Thermal destabilization of rhodopsin and opsin by proteolytic cleavage in bovine rod outer segment disk membranes. Biochemistry 40, 11176 11183.
25. Andersson, A. L. Maler (2005) Magnetic resonance investigations of lipid motion in isotropic bicelles. Langmuir 21, 7702 7709.
26. Ruprecht, J. J., T. Mielke, R. Vogel, C. Villa G. F. Schertler (2004) Electron crystallography reveals the structure of metarhodopsin I. EMBO J. 23, 3609 3620.
27. Albert, A. D., J. E. Young P. L. Yeagle (1996) Rhodopsin-cholesterol interactions in bovine rod outer segment disk membranes. Biochim. Biophys. Acta 1285, 47 55.
28. Huang, K. S., H. Bayley H. G. Khorana (1980) Delipidation of bacteriorhodopsin and reconstitution with exogenous phospholipid. Proc. Natl Acad. Sci. USA 77, 323 327.
29. Chen, G. Q. E. Gouaux (1999) Probing the folding and unfolding of wild-type and mutant forms of bacteriorhodopsin in micellar solutions: Evaluation of reversible unfolding conditions. Biochemistry 38, 15380 15387.
30. Nagy, J. K., W. L. Lonzer C. R. Sanders (2001) Kinetic study of folding and misfolding of diacylglycerol kinase in model membranes. Biochemistry 40, 8971 8980.
31. Baneres, J. L., A. Martin, P. Hullot, J. P. Girard, J. C. Rossi J. Parello (2003) Structure-based analysis of GPCR function: Conformational adaptation of both agonist and receptor upon leukotriene B4 binding to recombinant BLT1. J. Mol. Biol. 329, 801 814.
32. Karnik, S. S. H. G. Khorana (1990) Assembly of functional rhodopsin requires a disulfide bond between cysteine residues 110 and 187. J. Biol. Chem. 265, 17520 17524.
33. Doi, T., R. S. Molday H. G. Khorana (1990) Role of the intradiscal domain in rhodopsin assembly and function. Proc. Natl Acad. Sci. USA 87, 4991 4995.
34. Hwa, J., P. Garriga, X. Liu H. G. Khorana (1997) Structure and function in rhodopsin: Packing of the helices in the transmembrane domain and folding to a tertiary structure in the intradiscal domain are coupled. Proc. Natl Acad. Sci. USA 94, 10571 10576.
35. Rader, A. J., G. Anderson, B. Isin, H. G. Khorana, I. Bahar J. Klein-Seetharaman (2004) Identification of core amino acids stabilizing rhodopsin. Proc. Natl Acad. Sci. USA 101, 7246 7251.
36. Tastan, O., E. Yu, M. Ganapathiraju, A. Aref, A. Rader J. Klein-Seetharaman (2007) Comparison of stability predictions and simulated unfolding of rhodopsin structures. Photochem. Photobiol. 83, 351 362.
37. Tanuj Sapra, K., P. S. Park, S. Filipek, A. Engel, D. J. Muller K. Palczewski (2006) Detecting molecular interactions that stabilize native bovine rhodopsin. J. Mol. Biol. 358, 255 269.