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THE PLANT CELL, Vol 1, Issue 8 765-773, Copyright © 1989 by American Society of Plant Biologists
Oat Phytochrome Is Biologically Active in Transgenic Tomatoes
M. T. Boylan and P. H. Quail
United States Department of Agriculture/University of California, Berkeley, Plant Gene Expression Center, 800 Buchanan Street, Albany, California 94710
To determine the functional homology between phytochromes from
evolutionarily divergent species, we used the cauliflower mosaic virus 35S
promoter to express a monocot (oat) phytochrome cDNA in a dicot plant
(tomato). Immunoblot analysis shows that more than 50% of the transgenic
tomato plants synthesize the full-length oat phytochrome polypeptide.
Moreover, leaves of light-grown transgenic plants contain appreciably less
oat phytochrome than leaves from dark-adapted plants, and etiolated R1
transgenic seedlings have higher levels of spectrally active phytochrome
than wild-type tomato seedlings in direct proportion to the level of
immunochemically detectable oat polypeptide present. These data suggest
that the heterologous oat polypeptide carries a functional chromophore,
allowing reversible photoconversion between the two forms of the molecule,
and that the far-red absorbing form (Pfr) is recognized and selectively
degraded by the Pfr-specific degradative machinery in the dicot cell. The
overexpression of oat phytochrome has pleiotropic, phenotypic consequences
at all major phases of the life cycle. Adult transgenic tomato plants
expressing high levels of the oat protein tend to be dwarfed, with dark
green foliage and fruits. R1 transgenic seedlings have short hypocotyls
with elevated anthocyanin contents. We conclude that a monocot phytochrome
can be synthesized and correctly processed to a biologically active form in
a dicot cell, and that the transduction pathway components that interact
with the photoreceptor are evolutionarily conserved.
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