Uridine 5'-diphospho-glucose-4-epimerase (UDP-Glc epimerase) catalyses
the reversible epimerization of UDP-galactose and UDP-glucose. In con
trast to bacteria and yeast, expression of the UDP-Glc epimerase gene
in Arabidopsis was found not to be induced by galactose. To elucidate
the metabolic role of this enzyme, transgenic Arabidopsis plants expre
ssing the respective cDNA in sense or antisense orientation were const
ructed, leading to a range of plant lines with different UDP-Glc epime
rase activities. No alterations in morphology were observed and the re
lative amounts of different galactose-containing compounds were not af
fected if the plants were raised on soil. However, on agar plates in t
he presence of galactose, the growth of different lines was increasing
ly repressed with decreasing enzyme activity, and an increase in the U
DP-Gal content was observed in parallel, whereas the UDP-Glc content w
as nearly constant. The amount of galactose in the cell wall was incre
ased in plants with low UDP-Glc epimerase activity grown on galactose,
whereas the cellulose content in the leaves was not altered. Furtherm
ore, starch determined at different times of the day was highly abunda
nt in plants with low UDP-Glc epimerase activity in the presence of ga
lactose. It is proposed that low endogenous UDP-Glc epimerase activity
is responsible for the galactose toxicity of the wild-type. Possible
mech anisms by which the starch content might be modulated are discuss
ed.