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THE PLANT CELL, Vol 8, Issue 1 55-67, Copyright © 1996 by American Society of Plant Biologists
The Phytochrome-Deficient pcd1 Mutant of Pea Is Unable to Convert Heme to Biliverdin IX[alpha]
J. L. Weller, M. J. Terry, C. Rameau, J. B. Reid and R. E. Kendrick
Department of Plant Science, University of Tasmania, GPO Box 252C, Hobart, Tasmania 7001, Australia
We isolated a new pea mutant that was selected on the basis of pale color
and elongated internodes in a screen under white light. The mutant was
designated pcd1 for phytochrome chromophore deficient. Light-grown pcd1
plants have yellow-green foliage with a reduced chlorophyll (Chl) content
and an abnormally high Chl a/Chl b ratio. Etiolated pcd1 seedlings are
developmentally insensitive to far-red light, show a reduced response to
red light, and have no spectrophotometrically detectable phytochrome. The
phytochrome A apoprotein is present at the wild-type level in etiolated
pcd1 seedlings but is not depleted by red light treatment. Crude
phytochrome preparations from etiolated pcd1 tissue also lack spectral
activity but can be assembled with phycocyanobilin, an analog of the
endogenous phytochrome chromophore phytochromobilin, to yield a difference
spectrum characteristic of an apophytochrome-phycocyanobilin adduct. These
results indicate that the pcd1-conferred phenotype results from a
deficiency in phytochrome chromophore synthesis. Furthermore, etioplast
preparations from pcd1 seedlings can metabolize biliverdin (BV) IX[alpha]
but not heme to phytochromobilin, indicating that pcd1 plants are severely
impaired in their ability to convert heme to BV IX[alpha]. This provides
clear evidence that the conversion of heme to BV IX[alpha] is an enzymatic
process in higher plants and that it is required for synthesis of the
phytochrome chromophore and hence for normal photomorphogenesis.
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