Characterization of a novel aphid prenyltransferase displaying dual geranyl/farnesyl diphosphate synthase activity.
We report on the cDNA cloning and characterization of a novel short-chain isoprenyl diphosphate synthase from the aphid Myzus persicae. Of the three IPPS cDNAs we cloned, two yielded prenyltransferase activity following expression in Escherichia coli; these cDNAs encode identical proteins except for the presence, in one of them, of an N-terminal mitochondrial targeting peptide. Although the aphid enzyme was predicted to be a farnesyl diphosphate synthase by BLASTP analysis, rMpIPPS, when isopentenyl diphosphate and dimethylallyl diphosphate are supplied as substrates, typically generated geranyl diphosphate (C10) as its main product, along with significant quantities of farnesyl diphosphate (C15). Analysis of an MpIPPS homology model pointed to substitutions that could confer GPP/FPP synthase activity to the aphid enzyme.
Vandermoten
Sophie
S
Gembloux Agricultural University, Department of Functional and Evolutionary Entomology, Passage des Déportés 2, B-5030 Gembloux, Belgium. entomologie@fsagx.ac.be <entomologie@fsagx.ac.be>
Charloteaux
Benoit
B
Santini
Sébastien
S
Sen
Stephanie E
SE
Béliveau
Catherine
C
Vandenbol
Micheline
M
Francis
Frédéric
F
Brasseur
Robert
R
Cusson
Michel
M
Haubruge
Eric
E
D000818:Animals; D001042:Aphids / Q000201:enzymology* / Q000235:genetics; D003001:Cloning, Molecular; D004122:Dimethylallyltranstransferase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics; D051228:Geranyltranstransferase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D019476:Insect Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011487:Protein Conformation; D016415:Sequence Alignment
D019476:Insect Proteins; D004122:Dimethylallyltranstransferase; D051228:Geranyltranstransferase