Intermediates in the folding of the membrane protein bacteriorhodopsin
作者： Paula J. Booth , Sabine L. Flitsch , Lawrence J. Stern , Duncan A. Greenhalgh , Peter S. Kim
DOI: 10.1038/NSB0295-139
关键词:
摘要: Assembly of proteins within lipid bilayers is essential for the biogenesis and function biological membranes. Little known, however, about underlying mechanism assembly, it not clear whether possible to observe individual folding steps integral membrane either in vivo or vitro. Fluorescence spectroscopy used here follow time course events bacteriorhodopsin mixed detergent/lipid micelles. Transient folding-intermediates are detected binding retinal chromophore occurs at a late stage, when binds an apoprotein intermediate.
nature.com
sci-hub.se 参考文章(32)
H G Khorana, Bacteriorhodopsin, a membrane protein that uses light to translocate protons. Journal of Biological Chemistry. ,vol. 263, pp. 7439- 7442 ,(1988) , 10.1016/S0021-9258(18)68514-X
Dieter Oesterhelt, Walther Stoeckenius, Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane Methods in Enzymology. ,vol. 31, pp. 667- 678 ,(1974) , 10.1016/0076-6879(74)31072-5
E London, H G Khorana, Denaturation and renaturation of bacteriorhodopsin in detergents and lipid-detergent mixtures. Journal of Biological Chemistry. ,vol. 257, pp. 7003- 7011 ,(1982) , 10.1016/S0021-9258(18)34529-0
M J Liao, E London, H G Khorana, Regeneration of the native bacteriorhodopsin structure from two chymotryptic fragments. Journal of Biological Chemistry. ,vol. 258, pp. 9949- 9955 ,(1983) , 10.1016/S0021-9258(17)44589-3
K.S. Huang, H. Bayley, M.J. Liao, E. London, H.G. Khorana, Refolding of an integral membrane protein. Denaturation, renaturation, and reconstitution of intact bacteriorhodopsin and two proteolytic fragments. Journal of Biological Chemistry. ,vol. 256, pp. 3802- 3809 ,(1981) , 10.1016/S0021-9258(19)69526-8
Jean-Luc Popot, Sue-Ellen Gerchman, Donald M. Engelman, Refolding of bacteriorhodopsin in lipid bilayers: A thermodynamically controlled two-stage process Journal of Molecular Biology. ,vol. 198, pp. 655- 676 ,(1987) , 10.1016/0022-2836(87)90208-7
D.A. Greenhalgh, D.L. Farrens, S Subramaniam, H.G. Khorana, Hydrophobic amino acids in the retinal-binding pocket of bacteriorhodopsin Journal of Biological Chemistry. ,vol. 268, pp. 20305- 20311 ,(1993) , 10.1016/S0021-9258(20)80729-7
D.A. Greenhalgh, S Subramaniam, U Alexiev, H Otto, M.P. Heyn, H.G. Khorana, Effect of introducing different carboxylate-containing side chains at position 85 on chromophore formation and proton transport in bacteriorhodopsin. Journal of Biological Chemistry. ,vol. 267, pp. 25734- 25738 ,(1992) , 10.1016/S0021-9258(18)35669-2
M S Braiman, L J Stern, B H Chao, H G Khorana, Structure-function studies on bacteriorhodopsin. IV. Purification and renaturation of bacterio-opsin polypeptide expressed in Escherichia coli. Journal of Biological Chemistry. ,vol. 262, pp. 9271- 9276 ,(1987) , 10.1016/S0021-9258(18)48076-3
T Mogi, L J Stern, B H Chao, H G Khorana, Structure-function studies on bacteriorhodopsin. VIII. Substitutions of the membrane-embedded prolines 50, 91, and 186: the effects are determined by the substituting amino acids. Journal of Biological Chemistry. ,vol. 264, pp. 14192- 14196 ,(1989) , 10.1016/S0021-9258(18)71661-X