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Primary structure of gamma subunit precursor of calf muscle acetylcholine receptor deduced from the complementary dna sequence



Primary structure of gamma subunit precursor of calf muscle acetylcholine receptor deduced from the complementary dna sequence



European Journal of Biochemistry 143(1): 109-116



Clones carrying c[complementary]DNA sequences for the .gamma. subunit precursor of the acetylcholine receptor from calf skeletal muscle were isolated. Nucleotide sequence analysis of the cloned cDNA revealed the primary structure of this polypeptide, which consists of 519 amino acids including a hydrophobic prepeptide of 22 amino acids. The .gamma. subunit of the calf muscle acetylcholine receptor, like the .alpha. subunit of the calf as well as the human muscle receptor, shares features characteristic of all 4 subunits of the Torpedo californica electroplax receptor, such as the putative disulfide bridge corresponding to that in the .alpha. subunit proposed as being in close proximity to the acetylcholine binding site and the 4 putative, hydrophobic transmembrane segments M1-M4. Thus, the calf .gamma. subunit molecule apparently exhibits the same transmembrane topology as proposed for the fish receptor subunits. The degree of sequence homology between the calf and Torpedo .gamma. subunits (56%) is lower than that between the .alpha. subunits of the 2 spp. (81%). Some regions of the .gamma. subunit molecule, including the region encompassing the putative disulfide bridge and the region containing the putative transmembrane segments M1, M2 and M3, are relatively well conserved between the 2 spp.

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Accession: 006184877

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