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Science 14 March 1986:
Vol. 231. no. 4743, pp. 1284 - 1287
DOI: 10.1126/science.3511531
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Articles

Science, Vol 231, Issue 4743, 1284-1287
Copyright © 1986 by American Association for the Advancement of Science

articles

Biosynthesis of the Torpedo californica acetylcholine receptor alpha subunit in yeast

N Fujita, N Nelson, TD Fox, T Claudio, J Lindstrom, H Riezman, and GP Hess

Yeast cells were transformed with a plasmid containing complementary DNA encoding the alpha subunit of the Torpedo californica acetylcholine receptor. These cells synthesized a protein that had the expected molecular weight, antigenic specificity, and ligand-binding properties of the alpha subunit. The subunit was inserted into the yeast plasma membrane, demonstrating that yeast has the apparatus to express a membrane-bound receptor protein and to insert such a foreign protein into its plasma membrane. The alpha subunit constituted approximately 1 percent of the total yeast membrane. The alpha subunit constituted approximately 1 percent of the total yeast membrane proteins, and its density was about the same in the plasma membrane of yeast and in the receptor-rich electric organ of Electrophorus electricus. In view of the available technology for obtaining large quantities of yeast proteins, it may now be possible to obtain amplified amounts of interesting membrane-bound proteins for physical and biochemical studies.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Expression of Soluble Ligand- and Antibody-binding Extracellular Domain of Human Muscle Acetylcholine Receptor alpha Subunit in Yeast Pichia pastoris. ROLE OF GLYCOSYLATION IN alpha -BUNGAROTOXIN BINDING.
L. Psaridi-Linardaki, A. Mamalaki, M. Remoundos, and S. J. Tzartos (2002)
J. Biol. Chem. 277, 26980-26986
   Abstract »    Full Text »    PDF »
Yeast Expression and NMR Analysis of the Extracellular Domain of Muscle Nicotinic Acetylcholine Receptor alpha Subunit.
Y. Yao, J. Wang, N. Viroonchatapan, A. Samson, J. Chill, E. Rothe, J. Anglister, and Z.-Z. Wang (2002)
J. Biol. Chem. 277, 12613-12621
   Abstract »    Full Text »    PDF »
Correction for vol. 93, p. 11482.
(1997)
PNAS 94, 3481
   Full Text »
Heterologous expression of excitability proteins: route to more specific drugs?.
H. Lester (1988)
Science 241, 1057-1063
   Abstract »    PDF »
Ion Channels in Paramecium, Yeast, and Escherichia coli.
Y. Saimi, B. Martinac, M.C. Gustin, M.R. Culbertson, J. Adler, and C. Kung (1988)
Cold Spring Harb Symp Quant Biol 53, 667-673
   Abstract »    PDF »
Genetic reconstitution of functional acetylcholine receptor channels in mouse fibroblasts.
T Claudio, W. Green, D. Hartman, D Hayden, H. Paulson, F. Sigworth, S. Sine, and A Swedlund (1987)
Science 238, 1688-1694
   Abstract »    PDF »
Structure, function, and assembly of membrane proteins.
E Racker (1987)
Science 235, 959-961
   PDF »
Ion channels in yeast.
M. Gustin, B Martinac, Y Saimi, M. Culbertson, and C Kung (1986)
Science 233, 1195-1197
   Abstract »    PDF »


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