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Plant Cell, Vol. 11, 2303-2316, December 1999, Copyright © 1999, American Society of Plant Physiologists
Meristem-Localized Inducible Expression of a UDP-Glycosyltransferase Gene Is Essential for Growth and Development in Pea and Alfalfa
Ho-Hyung Wooa,b,
Marc J. Orbacha,
Ann M. Hirschb, and
Martha C. Hawesa
a Department of Plant Pathology, University of Arizona, Tucson, Arizona 85721
b Department of Molecular, Cell and Developmental Biology, University of California, Los Angeles, California 90095-1606
Correspondence to:
Martha C. Hawes, mhawes{at}u.arizona.edu (E-mail), 520-621-9290 (fax)
PsUGT1, which encodes a microsomal UDP-glucuronosyltransferase, was cloned from root tips of Pisum sativum. PsUGT1 expression is correlated with mitosis and strongly induced in dividing cells. A region at the C terminus of the encoded protein is closely related to the UDPglucuronic acid binding site consensus sequence, and the protein encoded by PsUGT1 catalyzes conjugation of UDPglucuronic acid to an unknown compound. Overexpression of PsUGT1 sense mRNA has no detectable effect on transgenic pea hairy root cultures or regenerated alfalfa. However, inhibiting PsUGT1 expression by the constitutive expression of antisense mRNA (under the control of the cauliflower mosaic virus 35S promoter) markedly retards growth and development of transgenic alfalfa. Cell structure and organization in the antisense plants are similar to those of controls, but plant growth is reduced and development is delayed. This inhibition in growth is correlated with a twofold delay in the time required for completion of a cell cycle and with a >99% inhibition of border cell production. Inhibition of PsUGT1 expression by meristem-localized inducible expression of PsUGT1 antisense mRNA (under the control of its own promoter) is lethal both in pea hairy roots and in transgenic alfalfa plants. These results indicate that PsUGT1 expression is required for normal plant growth and development, and they are consistent with the hypothesis that this UDP-glycosyltransferase regulates activity of a ligand(s) needed for cell division.
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