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Science 14 August 1987:
Vol. 237. no. 4816, pp. 744 - 749
DOI: 10.1126/science.2441469
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Articles

Science, Vol 237, Issue 4816, 744-749
Copyright © 1987 by American Association for the Advancement of Science

articles

Genomic organization and deduced amino acid sequence of a putative sodium channel gene in Drosophila

L Salkoff, A Butler, A Wei, N Scavarda, K Giffen, C Ifune, R Goodman, and G Mandel

The deduced amino acid sequence of a Drosophila gene isolated with a vertebrate sodium channel complementary DNA probe revealed an organization virtually identical to the vertebrate sodium channel protein; four homologous domains containing all putative membrane-spanning regions are repeated in tandem with connecting linkers of various sizes. All areas of the protein presumed to be critical for channel function show high evolutionary conservation. These include those proposed to function in voltage-sensitive gating, inactivation, and ion selectivity. All 24 putative gating charges of the vertebrate protein are in identical positions in the Drosophila gene. Ten introns interrupt the coding regions of the four homology units; introns with positions conserved among homology units bracket a region hypothesized to be the selectivity filter for the channel. The Drosophila gene maps to the right arm of the second chromosome in region 60D-E. This position does not coincide with any known mutations that confer behavioral phenotypes, but is close to the seizure locus (60A-B), which has been hypothesized to code for a voltage-sensitive sodium channel.


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