ISOLATION AND STRUCTURE OF AN ARRESTIN GENE FROM DROSOPHILA

被引:123
作者
SMITH, DP
SHIEH, BH
ZUKER, CS
机构
[1] UNIV CALIF SAN DIEGO,DEPT BIOL,LA JOLLA,CA 92093
[2] UNIV CALIF SAN DIEGO,CTR MOLEC GENET,LA JOLLA,CA 92093
关键词
Desensitization; Guanine nucleotide-binding protein; Phototransduction; Vision;
D O I
10.1073/pnas.87.3.1003
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
A Drosophila gene encoding a homologue of vertebrate arrestin was isolated by subtractive hybridization and identified as a member of a set of genes that are preferentially expressed in the visual system. This gene encodes a 364-amino acid protein that displays >40% amino acid sequence identity with human and bovine arrestin. Interestingly, the Drosophila homologue lacks the C-terminal sequences that were postulated to interact with rhodopsin during the quenching of the phototransduction cascade in the vertebrate visual response. These findings are discussed in terms of invertebrate phototransduction. The Drosophila gene was mapped cytogenetically to chromosomal position 36D1-2, near the ninaD locus. However, the arrestin gene does not appear to be the ninaD locus, as sequence analysis of three ethylmethane sulfate-induced ninaD mutant alleles reveals no alteration in amino acid sequence.
引用
收藏
页码:1003 / 1007
页数:5
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