Isolation and structure of an arrestin gene from Drosophila

Dean P. Smith, Bih Hwa Shieh, Charles S. Zuker

Research output: Contribution to journalArticle

109 Citations (Scopus)

Abstract

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.

Original languageEnglish (US)
Pages (from-to)1003-1007
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume87
Issue number3
StatePublished - 1990

Fingerprint

Arrestin
Drosophila
Light Signal Transduction
Genes
Vertebrates
Amino Acid Sequence
Rhodopsin
Invertebrates
Sulfates
Sequence Analysis
Alleles
Amino Acids
Proteins

Keywords

  • Desensitization
  • Guanine nucleotide-binding protein
  • Phototransduction
  • Vision

ASJC Scopus subject areas

  • Genetics
  • General

Cite this

Isolation and structure of an arrestin gene from Drosophila. / Smith, Dean P.; Shieh, Bih Hwa; Zuker, Charles S.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 87, No. 3, 1990, p. 1003-1007.

Research output: Contribution to journalArticle

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