A single-residue deletion alters the lipid selectivity of a K+ channel- associated peptide in the β-conformation: Spin label electron spin resonance studies

Biophysical Journal

Volumn 73, Issue 5, 1997, Pages 2588-2594

  Horváth, László I ^a,c   Knowles, Peter F ^b   Kovachev, Peter ^b   Findlay, John B C ^b   Marsh, Derek ^a  

^a MAX PLANCK INSTITUTE FOR BIOPHYSICAL CHEMISTRY   (Germany)

^b UNIVERSITY OF LEEDS   (United Kingdom)

^c INSTITUTE OF BIOCHEMISTRY   (Hungary)

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN; POTASSIUM CHANNEL;

ARTICLE; BINDING AFFINITY; CHANNEL GATING; CONFORMATIONAL TRANSITION; DELETION MUTANT; ELECTRON SPIN RESONANCE; MOLECULAR INTERACTION; PROTEIN ASSEMBLY; PROTEIN CONFORMATION; PROTEIN LIPID INTERACTION;

EID: 0342601419     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(97)78288-2     Document Type: Article

References (42)

1. Abramovitch, D. A., D. March, and G. L. Powell. 1990. Activation of beef heart cytochrome oxidate by cardiolipin and analogues of cardiolipin. Biochim. Biophys. Acta. 1020:34-42.
2. Kggeli, A., N. Boden, Y.-L. Chen, J. B. C. Findlay, P. F. Knowles, P. Kovatchev, P. J. M. Turnbull, L. I. Horváth, and D. Marsh. 1996. Peptides modelled on the transmembrane region of the slow voltage-gated isK potassium channel: structural characterisation of peptide assemblies in the β-strand conformation. Biochemistry. 33:16213-16221.
3. - channels. Nature. 365:850-852.
4. Ben-Efraim, I., D. Bach, and Y. Shai. 1993. Spcctroscopic and functional characterization of the putative transmembrane segment of the minK potassium channel. Biochemistry. 32:2371-2377.
5. Ben-Efraim, I., J. Strahilevitz, D. Bach, and Y. Shai. 1994. Secondary structure and membrane localisation of synthetic segments and a truncated form of the IsK (minK) protein. Biochemistry. 33:6966-6973.
6. Bogusz, S., A. Boxer, and D. D. Busath. 1992. An SS1-SS2 β-barrel structure for the voltage-activated potassium channel. Protein Eng. 3:285-293.
7. Brophy, P. J. 1977. Association of proteolipid apoproteins from bovine myelln with phosphollpid in bilayer vesicles. FEBS Lett. 84:92-96.
8. Brotherus, J. R., O. H. Griffith, M. O. Bratherus, P. C. Josi, J. R. Silvius, and L. E. Hokin. 1981. Lipid-protein multiple binding equilibria in membranes. Biochemistry. 20:3261-3267.
9. Byler, D. M., and H. Susi. 1986. Examination of the secondary structure of proteins by deconvoluted FT1R spectra. Biopolymers. 25:469-487.
10. Cornea, R. L., L. R. Jones, J. M. Autry, and D. D. Thomas. 1997. Mutation and phosphorylation change the oligomeric structure of phospholamban in lipid bilayers. Biochemistry. 36:2960-2967.
11. Durrell, S. R., and H. R. Guy. 1992. Atomic scale structure and functional models of voltage-gated potassium channels. Biophys. J. 62:238-250.
12. Eibl, H., and W. E. M. Lands. 1969. A new, sensitive determination of phosphate. Anal. Biochem. 30:51-57.
13. Eisenberg, D., Schwarz, E., Komaromy, M., and Wall, R. 1984. Analysis of membrane and surface protein sequences with the hydrophobic moment plot. J. Mol. Biol. 179:125-142.
14. +-ATPase membranes from Squalus acanthias. Biochemistry. 24:3572-3578.
15. + channel alter ion selectivity and open-channel block. Neuron. 7:403-408.
16. Guy, H. R., and F. Conti. 1990. Pursuing the structure and function of voltage-gated channels. Trends Neurosci. 13:201-206.
17. + channel In mouse heart. EMBO J. 10:2805-2811.
18. Horváth, L. I., P. J. Brophy, and D. Marsh. 1988. Influence of lipid headgroup on the specificity and exchange dynamics in lipid-protein interactions. A spin label study of myelin proteolipld apoprotein-phospholipid complexes. Biochemistry. 27:5296-5304.
19. + channel-associated peptide in a lipid bilayer: conformation, lipid-proteln interactions, and rotational diffusion. Biochemistry. 34:3893-3898.
20. King, D. S., C. G. Fields, and G. B. Fields. 1990. A cleavage method which minimizes side reactions following Fmoc solid phase peptide synthesis. Int. J. Pept. Protein Res. 36:255-266.
21. Kusumi, A., and J. S. Hyde. 1982. Spin-label saturation-transfer electron spin resonance detection of transient association of rhodopsin in reconstituted membranes. Biochemistry. 21:5978-5983.
22. Lowry, O. H., N. J. Rosebrough, A. C. Farr, and R. J. Randall. 1951. Protein measurement with the Polin phenol reagent. J. Biol. Chem. 193:265-275.
23. Marsh, D. 1982. Electron spin resonance: spin label probes. In Techniques in Lipid and Membrane Biochemistry, Vol. B4/II, B426, J. C. Metcalfe and T. R. Hesketh, editors. Elsevier, Amsterdam, 1-44.
24. Marsh, D. 1985. ESR spin label studies of lipid-protein interactions. In Progress in Protein-Lipid Interactions, Vol. 1. A. Watts and J. J. H. H. M. De Pont, editors. Elsevier, Amsterdam. 143-172.
25. Marsh, D. 1990. Handbook of Lipid Bilayers, CRC Press, Boca Raton, FL.
26. Marsh, D. 1993. The nature of the lipid-protein interface and the influence of protein structure on protein-lipid interactions. In New Comprehensive Biochemistry: Protein-Lipid Interactions, Ch. 2. A. Watts, editor. Elsevier, Amsterdam. 41-66.
27. Marsh, D. 1996. Peptide models for membrane channels. Biochem. J. 315:345-361.
28. Marsh, D. 1997a. Stoichiometry of lipid-protein interaction and integral membrane protein structure. Eur. Biophys. J. 26:203-208.
29. Marsh, D. 1997b. Dichroic ratios in polarized Fourier transform infrared for nonaxial symmetry of β-sheet structures. Biophys. J. 72:2710-2718.
30. Marsh, D., and A. Watts. 1982. Spin-labeling and lipid-protein interactions in membranes. In Lipid-Protein Interactions, Vol. II. P. C. Jost and O. H. Griffith, editors. Wiley-Interscience, New York. 53-126.
31. Murai, T., A. Kakizuka., T. Takumi, H. Ohkubo, and S. Nakanishi. 1989. Molecular cloning and sequence analysis of human genomic DNA encoding a novel membrane protein which exhibits a slowly activating potassium channel activity. Biochem. Biophys. Res. Commun. 161:176-181.
32. Peelen, S. J. C. J., J. C. Sanders, M. A. Hemminga, and D. Marsh. 1992. Stoichiometry, selectivity, and exchange dynamics of lipid-protein interaction with bacteriophage M13 coat protein studied by spin label electron spin resonance. Effects of protein secondary structure. Biochemistry. 31:2670-2677.
33. Ryba, N. J. P., and D. Marsh. 1992. Protein rotational diffusion and lipid/protein interactions in recombinants of bovine rhodopsin with saturated diacylphosphatidylcholines of different chain lengths studied by conventional and saturation transfer electron spin resonance. Biochemistry. 31:7511-7518.
34. Ryba, N. J. P., D. Marsh, and R. Uhl. 1993. The kinetics and thermodynamics of bleaching of rhodopsin in dimyristoylphosphatidylcholine. Identification of meta-I, meta-II, and meta-III intermediates. Biophys. J. 64:1801-1812.
35. - currents in Xenopus oocytes. Biophys. J. 68:A204.
36. Spruijt, R. B., and M. A. Hemminga. 1991. The in situ aggregational and conformational state of the major coat protein of bacteriophage M13 in phospholipid bilayers mimicking the inner membrane of host Escherichia coli. Biochemistry. 30:11147-11154.
37. Spruijt, R. B., C. J. A. M. Wolfs, and M. A. Hemminga. 1989. Aggregation-related conformational change of the membrane-associated coat protein of bacteriophage M13. Biochemistry. 28:9158-9165.
38. sK potassium channel. J. Biol. Chem 266:22192-22198.
39. Takumi, T., H. Ohkubo, and S. Nakanishi. 1988. Cloning of a membrane protein that induces a slow voltage-gated potassium current. Science. 242:1042-1045.
40. + channel subunits is extended. Biophys. J. 72:A351.
41. Tzounopoulos, T., J. Maylie, and J. P. Edelman. 1995. Induction of endogeneous channels by high levels of heterologous membrane proteins in Xenopus oocytes. Biophys. J. 69:904-908.
42. Wolfs, C. J. A. M., L. I. Horváth, D. Marsh, A. Watts, and M. A. Hemminga. 1989. Spin-label BSR of bacteriophage M13 coat protein in mixed lipid bilayers. Characterization of molecular selectivity of charged phospholipids for the bacteriophage coat protein in lipid bilayers. Biochemistry. 28:9995-10001.