Open AccessExpression pattern in the antennae of a newly isolated lepidopteran Gq protein α subunit cDNA
Author(s) -
JacquinJoly Emmanuelle,
François MarieChristine,
Burnet Michael,
Lucas Philippe,
Bourrat Franck,
Maida Rosario
Publication year - 2002
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1046/j.1432-1033.2002.02863.x
Subject(s) - biology , complementary dna , protein subunit , peptide sequence , g protein , open reading frame , olfaction , g alpha subunit , signal transduction , microbiology and biotechnology , protein primary structure , biochemistry , gene , neuroscience
From the antennae of the moth Mamestra brassicae , we have identified a lepidopteran G protein α subunit belonging to the Gq family, through immunological detection in crude antennal extract and antennal primary cell cultures, followed by molecular cloning. The complete cDNA sequence (1540 bp) contains an open reading frame encoding a protein of 353 amino acids. This deduced sequence possesses all of the characteristics of the Gq family and shares a very high degree of amino‐acid sequence identity with vertebrate (80% with mouse or human Gqα) and invertebrate subunits (varying between 60 and 87% for Gqα from organisms as diverse as sponge and Drosophila ). The expression pattern of the Gq subunit in adult antennae was associated with the olfactory sensilla suggesting a specific role in olfaction. These data provide molecular evidence for a component of the phosphoinositide signaling pathway in moth antennae: this G protein α subunit may be involved in the olfaction transduction process through interaction with G‐protein‐coupled receptors, stimulating the phospholipase C mediated second messenger pathway.