Shima Y, Tada Y, Furuki M, Hara Y, Ohta H
Laboratory of Biochemistry, Kyorin University School of Health Sciences, Tokyo, Japan.
Biochem Biophys Res Commun. 1998 Jul 30;248(3):778-82. doi: 10.1006/bbrc.1998.8981.
The Na+,K(+)-ATPase activity of membranes from a behavioral mutant of C. elegans was found to be about one-third that of the wild-type. The levels of mRNA and polypeptide of Na+,K(+)-ATPase alpha-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 alpha-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.
秀丽隐杆线虫行为突变体的膜中钠钾ATP酶活性约为野生型的三分之一。突变体中钠钾ATP酶α亚基的mRNA和多肽水平与野生型一样高,但突变体线虫中钠钾ATP酶磷酸化中间体的水平比野生型低80%。在α亚基中参与磷酸化中间体形成的高度保守区域发现了一个预测的单氨基酸替换(亮氨酸替换为苯丙氨酸)。突变体线虫异常的进食行为可能归因于这种错义突变。