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Guayule plants accumulate large quantities of rubber within
parenchyma cells of their stembark tissues. This rubber is packed
within discrete organelles called rubber particles composed primarily
of a lipophilic, cis-polyisoprene core, small amounts of
lipids, and several proteins, the most abundant of which is the
M
Volume 270,
Number 15,
Issue of April 14, pp. 8487-8494, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
CHARACTERIZATION BASED ON cDNA CLONING AND SPECTROSCOPIC ANALYSIS
OF THE SOLUBILIZED ENZYME AND ITS REACTION PRODUCTS
53,000 rubber particle protein (RPP). We have
cloned and sequenced a full-length cDNA for RPP and show that it has
65% amino acid identity and 85% similarity to a cytochrome P450 known
as allene oxide synthase (AOS), recently identified from flaxseed. RPP
contains the same unusual heme-binding region and possesses a similar
defective I-helix region as AOS, suggesting an equivalent biochemical
function. Spectral analysis of solubilized RPP verifies it as a P450,
and enzymatic assays reveal that it also metabolizes
13( S)-hydroperoxy-(9 Z,11 E)-octadecadienoic
acid into the expected ketol fatty acids at rates comparable with
flaxseed AOS. RPP is unusual in that it lacks the amino-terminal
membrane anchor and the established organelle targeting sequences found
on other conventional P450s. Together, these factors place RPP in the
CYP74 family of P450s and establish it as the first P450 localized in
rubber particles and the first eukaryotic P450 to be identified outside
endoplasmic reticulum, mitochondria, or plastids.
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