Abstract

The Na+,K+-ATPase activity of membranes from a behavioral mutant ofC. eleganswas found to be about one-third that of the wild-type. The levels of mRNA and polypeptide of Na+,K+-ATPase α-subunit in the mutant were as high as those in the wild-type, but the level of the phosphorylated intermediate of the Na+,K+ATPase in the mutant worm was 80% lower than that in the wild-type. A single predicted amino acid replacement (Leu to Phe) was found in a highly conserved region in the α-subunit that is involved in the formation of phosphorylated intermediate. The abnormal feeding behavior of the mutant worm may be attributed to this missense mutation.

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