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THE PLANT CELL, Vol 9, Issue 8 1459-1467, Copyright © 1997 by American Society of Plant Biologists
Cloning and Expression of a Gibberellin 2[beta],3[beta]-Hydroxylase cDNA from Pumpkin Endosperm
T. Lange, S. Robatzek and A. Frisse
Albrecht-von-Haller-Institut fur Pflanzenwissenschaften, Universitat Gottingen, Untere Karspule 2, D-37073 Gottingen, Germany
A cDNA expression library in [lambda]MOSElox derived from poly(A)+ RNA from
pumpkin endosperm was screened immunologically with a polyclonal antibody
raised against partially purified gibberellin (GA)
2[beta],3[beta]-hydroxylase from pumpkin endosperm. A recombinant fusion
protein encoded by a selected positive clone catalyzed
3[beta]-hydroxylation of GA15, GA24, GA25, and GA17 and of GA12-aldehyde,
GA12, GA9, and GA20, albeit less efficiently. The fusion protein also
catalyzed 2[beta]-hydroxylation of the C20 GAs GA25, GA13, and, as
identified putatively, GA28. The full-length clone contains an open reading
frame of 1041 nucleotides encoding 346 amino acid residues with a predicted
molecular weight of 38,992 and pl of 7.2. Transcript levels of this gene
and of the previously cloned GA 7-oxidase and 20-oxidase genes from pumpkin
endosperm rose until day 2 after the start of imbibition of the mature
seeds, but only at one-two hundredth to one-six thousandth of the level
found in the endosperm, as determined by quantitative reverse
transcriptase-polymerase chain reaction. In contrast, GA 7-oxidase,
20-oxidase, and 3[beta]-hydroxylase enzyme activities were present in
cell-free systems prepared from embryos of mature seeds and decreased after
imbibition.
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