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THE PLANT CELL, Vol 3, Issue 7 719-735, Copyright © 1991 by American Society of Plant Biologists
Plant Enolase: Gene Structure, Expression, and Evolution
D. Van Der Straeten, R. A. Rodrigues-Pousada, H. M. Goodman and M. Van Montagu
Laboratorium voor Genetica, Rijksuniversiteit Gent, K.L. Ledeganckstraat 35, B-9000 Gent, Belgium
Enolase genes were cloned from tomato and Arabidopsis. Comparison of their
primary structures with other enolases revealed a remarkable degree of
conservation, except for the presence of an insertion of 5 amino acids
unique to plant enolases. Expression of the enolase genes was studied under
various conditions. Under normal growth conditions, steady-state messenger
and enzyme activity levels were significantly higher in roots than in green
tissue. Large inductions of mRNA, accompanied by a moderate increase in
enzyme activity, were obtained by an artificial ripening treatment in
tomato fruits. However, there was little effect of anaerobiosis on the
abundance of enolase messenger. In heat shock conditions, no induction of
enolase mRNA was observed. We also present evidence that, at least in
Arabidopsis, the hypothesis that there exists a complete set of glycolytic
enzymes in the chloroplast is not valid, and we propose instead the
occurrence of a substrate shuttle in Arabidopsis chloroplasts for
termination of the glycolytic cycle.
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