Revisiting the odorant‐binding protein LUSH of Drosophila melanogaster: evidence for odour recognition and discrimination

FEBS Letters

Pickett, John A¹  Pelosi, Paolo⁴  Zhang, Guo-An²  Birkett, Michael A¹  Field, Linda M¹  Zhou, Jing-Jiang¹  Huang, Wensheng³ 

[1] Rothamsted Research, Harpenden, Hertfordshire AL5 2JQ, UK;College of Sciences and Biotechnology, Huazhong Agricultural University, Wuhan, Hubei 430070, PR China;The GMOs Detection Laboratory, Animal and Plant Quarantine Institute, Beijing 100029, PR China;Dipartimento di Chimica e Biotecnologie Agrarie, University of Pisa, Via S. Michele, 26124 Pisa, Italy

关键词: Odorant-binding protein;    Chemical communication;    Fluorescence binding assay;    N-Phenylnaphthylamine;    Phthalate;    Drosophila melanogaster;    1-NPN;    N-phenylnaphthylamine;    OBP;    odorant-binding protein;    CSP;    chemosensory protein;   

DOI  :  10.1016/S0014-5793(03)01521-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

LUSH is a soluble odorant-binding protein of the fruit fly Drosophila melanogaster. Mutants not expressing this protein have been reported to lack the avoidance behaviour, exhibited by wild type flies, to high concentrations of ethanol. Very recently, the three-dimensional structure of LUSH complexed with short-chain alcohols has been resolved supporting a role for this protein in binding and detecting small alcohols. Here we report that LUSH does not bind ethanol and that wild type flies are in fact attracted by high concentrations of ethanol. We also report that LUSH binds some phthalates and that flies are repelled by such compounds. Finally, our fluorescence data, interpreted in the light of the three-dimensional structure of LUSH, indicate that the protein undergoes a major conformational change, similar to that reported for the pheromone-binding protein of Bombyx mori, but triggered, in our case, by ligand.

【 授权许可】

Unknown