« Previous AbstractThe odorant-binding proteins of Drosophila melanogaster: annotation and characterization of a divergent gene family    Next Abstract"Lag effects in the impacts of mass coral bleaching on coral reef fish, fisheries, and ecosystems" »

Mol Cell Proteomics

Title:		Characterization of a subfamily of beetle odorant-binding proteins found in hemolymph
Author(s):		Graham LA; Brewer D; Lajoie G; Davies PL;
Address:		"Department of Biochemistry, Queen's University, Kingston, Ontario K7L 3N6, Canada. grahamla@post.queensu.ca"
Journal Title:		Mol Cell Proteomics
Year:		2003
Volume:		20030725
Issue:		8
Page Number:		541 - 549
DOI:		10.1074/mcp.M300018-MCP200
ISSN/ISBN:		1535-9476 (Print) 1535-9476 (Linking)
Abstract:		"In insects, hydrophobic odorants are transported through the sensillar lymph to receptors on sensory neurons by odorant-binding proteins (OBPs). The beetle Tenebrio molitor, which is a pest of stored grain products, produces a set of 12-14-kDa OBP-like proteins in its hemolymph. The structure of one of these proteins and that of a moth pheromone-binding protein have been solved. Both proteins have at least six alpha-helices with an internal, hydrophobic, ligand-binding pocket, but the beetle OBP lacks one of the disulfide bonds immediately adjacent to this pocket. To explore this difference and to sample isoform diversity, T. molitor hemolymph OBPs were fractionated by size-exclusion chromatography and reversed-phase high performance liquid chromatography. Selected fractions were reduced and alkylated, and tryptic peptides were sequenced by tandem mass spectrometry. Partial sequences of 7 different isoforms were obtained and used to clone 9 new cDNAs encoding OBPs with identities from 32 to 99%. The more divergent isoforms have numerous substitutions of hydrophobic residues that presumably alter the shape and specificity of the ligand-binding pocket. These isoforms all lack the same third disulfide bridge and are more similar to one another than to any of the 38 OBPs in Drosophila melanogaster. They have presumably arisen via gene duplication following separation of the major insect orders"
Keywords:		"Amino Acid Sequence Animals Base Sequence Cloning, Molecular DNA, Complementary/genetics Hemolymph/metabolism Insect Proteins/*chemistry/genetics/isolation & purification Mass Spectrometry Molecular Sequence Data Odorants Phylogeny Protein Isoforms/chemis;"
Notes:		"MedlineGraham, Laurie A Brewer, Dyanne Lajoie, Gilles Davies, Peter L eng 2003/07/29 Mol Cell Proteomics. 2003 Aug; 2(8):541-9. doi: 10.1074/mcp.M300018-MCP200. Epub 2003 Jul 25"