First published online July 18, 2002; 10.1104/pp.002626
Plant Physiol, August 2002, Vol. 129, pp. 1866-1871
Redox Regulation of Arabidopsis
3-Deoxy-D-arabino-Heptulosonate 7-Phosphate
Synthase1
Robert
Entus,
Michael
Poling, and
Klaus M.
Herrmann*
Department of Biochemistry, Purdue University, West Lafayette,
Indiana 47907
The cDNA for
3-deoxy-D-arabino-heptulosonate 7-phosphate
synthase of Arabidopsis encodes a polypeptide with an amino-terminal signal sequence for plastid import. A cDNA fragment encoding the processed form of the enzyme was expressed in Escherichia
coli. The resulting protein was purified to electrophoretic
homogeneity. The enzyme requires Mn2+ and reduced
thioredoxin (TRX) for activity. Spinach (Spinacia oleracea) TRX f has an apparent dissociation
constant for the enzyme of about 0.2 µM. The
corresponding constant for TRX m is orders of magnitude
higher. In the absence of TRX, dithiothreitol partially activates the
enzyme. Upon alkylation of the enzyme with iodoacetamide, the
dependence on a reducing agent is lost. These results indicate that the
first enzyme in the shikimate pathway of Arabidopsis appears to be
regulated by the ferredoxin/TRX redox control of the chloroplast.
1
This is journal paper no. 16,461 of the Purdue
University Agricultural Experiment Station.
*
Corresponding author; e-mail herrmann{at}purdue.edu; fax
765-494-7897.
© 2002 American Society of Plant Physiologists
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