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Letters to Nature
Nature 301, 251 - 255 (20 January 1983); doi:10.1038/301251a0

Primary structures of β- and δ-subunit precursors of Torpedo californica acetylcholine receptor deduced from cDNA sequences

Masaharu Noda*, Hideo Takahashi*, Tsutomu Tanabe*, Mitsuyoshi Toyosato*, Sho Kikyotani*, Tadaaki Hirose, Michiko Asai, Hideaki Takashima, Seiichi Inayama, Takashi Miyata & Shosaku Numa*

*Department of Medical Chemistry, Kyoto University Faculty of Medicine, Kyoto 606, Japan
Pharmaceutical Institute, Keio University School of Medicine, Tokyo 160, Japan
Department of Biology, Kyushu University Faculty of Science, Fukuoka 812, Japan

The nicotinic acetylcholine receptor (AChR) from fish electric organ and mammalian skeletal muscle is the best characterized neurotransmitter receptor (reviewed in refs 1–3). The AChR from the electroplax of the ray Torpedo californica consists of five subunits present in a molar stoichiometry of α 2 βγδ (refs 4–6); the apparent molecular weights of the α-, β-, γ- and δ-subunits are 40,000 (40K), 50K, 60K and 65K, respectively7–11. Knowledge of the primary structures of these constituent polypeptides would facilitate the understanding of the molecular mechanism underlying the function of the neurotransmitter receptor. Recently, we have cloned cDNA for the α-subunit precursor of the T. californica AChR and have deduced the primary structure of this polypeptide from the nucleotide sequence of the cloned cDNA12. Here we report the cloning and nucleotide analysis of cDNAs for the AChR β- and δ-subunit precursors. The primary structures of the two polypeptides deduced from the cDNA sequences reveal conspicuous amino acid sequence homology among these and the α-subunits. The three subunits contain several highly conserved regions which may be essential for the receptor function or inter-summit interaction.

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