Two distinct forms of farnesyl diphosphate synthase (FPPS1 and FPPS2) have been cloned from the spruce budworm, but their function in insects is not well understood.  Because FPPS1 has an N-terminal extension that is predicted to target import into the mitochondria, several CfFPPS1 constructs were prepared, expressed and studied.  We determined that neither the full nor the truncated versions of FPPS1 were catalytically active; however, the addition of small amounts of FPPS2 to these samples appeared to stimulate activity.  Because it is known that these proteins form a heteromeric association, further studies were performed.  Secondary structure and stability of FPPS1, FPPS2, and FPPS1/FPPS2 combinations were evaluated by circular dichroism measurements.  While all samples showed similar secondary structure, they displayed distinct denaturation profiles, indicating that different higher order structures were present.  Native PAGE suggests that the addition of small amounts of FPPS2 to FPPS1 causes a change in protein aggregation.

Functional analysis of type 1 and type 2 FPPSs of the spruce budworm

243rd National Meeting (2012)

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