z-logo
open-access-imgOpen Access
Odorant Receptor C-Terminal Motifs in Divergent Insect Species
Author(s) -
Raymond R. Miller,
Zhijian Tu
Publication year - 2008
Publication title -
journal of insect science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.551
H-Index - 49
ISSN - 1536-2442
DOI - 10.1673/031.008.5301
Subject(s) - biology , drosophila melanogaster , receptor , melanogaster , olfaction , structural motif , genetics , insect , conserved sequence , transmembrane domain , g protein coupled receptor , peptide sequence , microbiology and biotechnology , evolutionary biology , gene , biochemistry , neuroscience , botany
Insect odorant receptors are a large family of seven transmembrane proteins believed to be G-protein coupled receptors. The peptide sequences of two odorant receptors within a given species may share as little as 17% identity, and there is limited similarity between receptors of divergent species. One exception is DmOr83b, which is found in Drosophila melanogaster and is highly conserved in at least ten other insect species. DmOr83b is broadly expressed in most of the olfactory sensory neurons of D. melanogaster at most developmental stages, while other odorant receptors tend to have more restricted and specific expression patterns. DmOr83b is critical for D. melanogaster olfaction, and it is involved in properly localizing other odorant receptors possibly by forming heterodimers with these receptors. The C-terminal region has been implicated as sites for such heterodimer formation. Multiple em for motif elicitation (MEME), a hidden markov model based program, was used to uncover three conserved motifs in the C-termini of a vast majority of the odorant receptor peptides from Anopheles gambiae , D. melanogaster , and Apis mellifera . These motifs are also found in DmOr83b and its orthologs and the order of these motifs is conserved as well. The conservation of these motifs among divergent odorant receptors in divergent species suggests functional importance. We propose that these motifs are involved in receptor- receptor protein interactions, contributing to the heterodimer formation between DmOr83b (or its orthologs) and other odorant receptors.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.
Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom