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Proc Natl Acad Sci U S A


Title:Isolation and functional expression of an animal geranyl diphosphate synthase and its role in bark beetle pheromone biosynthesis
Author(s):Gilg AB; Bearfield JC; Tittiger C; Welch WH; Blomquist GJ;
Address:"Department of Biochemistry and Molecular Biology, University of Nevada, Reno, NV 89557-0014, USA"
Journal Title:Proc Natl Acad Sci U S A
Year:2005
Volume:20050627
Issue:28
Page Number:9760 - 9765
DOI: 10.1073/pnas.0503277102
ISSN/ISBN:0027-8424 (Print) 1091-6490 (Electronic) 0027-8424 (Linking)
Abstract:"Geranyl diphosphate synthase (GPPS) catalyzes the condensation of dimethylallyl diphosphate and isopentenyl diphosphate to form geranyl diphosphate. Geranyl diphosphate is the precursor of monoterpenes, a large family of natural occurring C(10) compounds predominantly found in plants. Similar to plants but unique to animals, some bark beetle genera (Coleoptera: Scolytidae) produce monoterpenes that function in intraspecific chemical communication as aggregation and dispersion pheromones. The release of monoterpene aggregation pheromone mediates host colonization and mating. It has been debated whether these monoterpene pheromone components are derived de novo through the mevalonate pathway or result from simple modifications of dietary precursors. The data reported here provide conclusive evidence for de novo biosynthesis of monoterpene pheromone components from bark beetles. We describe GPPS in the midgut tissue of pheromone-producing male Ips pini. GPPS expression levels are regulated by juvenile hormone III, similar to other mevalonate pathway genes involved in pheromone biosynthesis. In addition, GPPS transcript is almost exclusively expressed in the anterior midgut of male I. pini, the site of aggregation pheromone biosynthesis. The recombinant enzyme was functionally expressed and produced geranyl diphosphate as its major product. The three-dimensional model structure of GPPS shows that the insect enzyme has the sequence structural motifs common to E-isoprenyl diphosphate synthases"
Keywords:"Alkyl and Aryl Transferases/genetics/*isolation & purification/*metabolism Amino Acid Sequence Animals Base Sequence Cloning, Molecular Cluster Analysis Coleoptera/*enzymology DNA Primers Digestive System/metabolism Gene Expression Profiling *Gene Express;"
Notes:"MedlineGilg, Anna B Bearfield, Jeremy C Tittiger, Claus Welch, William H Blomquist, Gary J eng Comparative Study Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. 2005/06/29 Proc Natl Acad Sci U S A. 2005 Jul 12; 102(28):9760-5. doi: 10.1073/pnas.0503277102. Epub 2005 Jun 27"

 
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