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Biochemical Characterization of Stromal and Thylakoid-Bound Isoforms of Isoprene Synthase in Willow Leaves1

Mary C. Wildermuth and Ray Fall*

Department of Chemistry and Biochemistry, and the Cooperative Institute for Research in Environmental Sciences, University of Colorado, Boulder, Colorado 80309-0215

Isoprene synthase is the enzyme responsible for the foliar emission of the hydrocarbon isoprene (2-methyl-1,3-butadiene) from many C3 plants. Previously, thylakoid-bound and soluble forms of isoprene synthase had been isolated separately, each from different plant species using different procedures. Here we describe the isolation of thylakoid-bound and soluble isoprene synthases from a single willow (Salix discolor L.) leaf-fractionation protocol. Willow leaf isoprene synthase appears to be plastidic, with whole-leaf and intact chloroplast fractionations yielding approximately equal soluble (i.e. stromal) and thylakoid-bound isoprene synthase activities. Although thylakoid-bound isoprene synthase is tightly bound to the thylakoid membrane (M.C. Wildermuth, R. Fall [1996] Plant Physiol 112: 171-182), it can be solubilized by pH 10.0 treatment. The solubilized thylakoid-bound and stromal isoprene synthases exhibit similar catalytic properties, and contain essential cysteine, histidine, and arginine residues, as do other isoprenoid synthases. In addition, two regulators of foliar isoprene emission, leaf age and light, do not alter the percentage of isoprene synthase activity in the bound or soluble form. The relationship between the isoprene synthase isoforms and the implications for function and regulation of isoprene production are discussed.

1   This research was supported by grants from the National Science Foundation (ATM-9312153 and ATM-9633285), the Southern Oxidants Study (North Carolina State University subcontract 91-0074-12), and the U.S. Environmental Protection Agency (R 825259-01-0). M.C.W. was also supported by the National Science Foundation Atmospheric Chemistry Traineeship (EAR-9256339).
*   Corresponding author; e-mail r.fall{at}colorado.edu; fax 1-303-492-1149.

Plant Physiol. (1998) 116: 1111-1123
Copyright Clearance Center:   0032-0889/98/116/1111/13
© 1998 American Society of Plant Physiologists




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