Bedoukian   RussellIPM   RussellIPM   Piezoelectric Micro-Sprayer


Home
Animal Taxa
Plant Taxa
Semiochemicals
Floral Compounds
Semiochemical Detail
Semiochemicals & Taxa
Synthesis
Control
Invasive spp.
References

Abstract

Guide

Alphascents
Pherobio
InsectScience
E-Econex
Counterpart-Semiochemicals
Print
Email to a Friend
Kindly Donate for The Pherobase

« Previous AbstractIndoor air pollution: a global health concern    Next AbstractHeadspace water-based liquid-phase microextraction »

Proc Natl Acad Sci U S A


Title:Evolving protein functional diversity in new genes of Drosophila
Author(s):Zhang J; Dean AM; Brunet F; Long M;
Address:"Department of Ecology and Evolution, University of Chicago, Chicago, IL 60637, USA"
Journal Title:Proc Natl Acad Sci U S A
Year:2004
Volume:20041108
Issue:46
Page Number:16246 - 16250
DOI: 10.1073/pnas.0407066101
ISSN/ISBN:0027-8424 (Print) 1091-6490 (Electronic) 0027-8424 (Linking)
Abstract:"The mechanism by which protein functional diversity expands is an important evolutionary issue. Studies of recently evolved chimeric genes permit direct investigation of the origin of new protein functions before they become obscured by subsequent evolution. Found in several African Drosophila species, jingwei (jgw), a recently evolved gene with a domain derived from the still extant short-chain alcohol dehydrogenase (ADH) through retroposition, provides an opportunity to examine this previously undescribed process directly. We expressed JGW proteins in a microbial expression system and, after purification, investigated their enzymatic properties. We found that, unexpectedly, positive Darwinian selection for amino acid replacements outside the active site of JGW produced a novel dehydrogenase with altered substrate specificity compared with the ancestral ADH. Instead of detoxifying and assimilating ethanol like its Adh parental gene, we observe that JGW efficiently utilizes long-chain primary alcohols found in hormone and pheromone metabolism. These data suggest that protein functional diversity can expand rapidly under the joint forces of exon shuffling, gene duplication, and natural selection"
Keywords:"Alcohol Dehydrogenase/genetics/physiology Amino Acid Sequence Amino Acid Substitution Animals Drosophila/*genetics/*physiology Drosophila Proteins/*genetics/*physiology Evolution, Molecular *Genes, Insect Models, Molecular Molecular Sequence Data Mutant C;"
Notes:"MedlineZhang, Jianming Dean, Antony M Brunet, Frederic Long, Manyuan eng Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. 2004/11/10 Proc Natl Acad Sci U S A. 2004 Nov 16; 101(46):16246-50. doi: 10.1073/pnas.0407066101. Epub 2004 Nov 8"

 
Back to top
 
Citation: El-Sayed AM 2024. The Pherobase: Database of Pheromones and Semiochemicals. <http://www.pherobase.com>.
© 2003-2024 The Pherobase - Extensive Database of Pheromones and Semiochemicals. Ashraf M. El-Sayed.
Page created on 25-11-2024