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Plant Physiol, April 2000, Vol. 122, pp. 1193-1200
The Plastidic Phosphoglucomutase from Arabidopsis. A
Reversible Enzyme Reaction with an Important Role in Metabolic
Control1
Cyril
Periappuram,
Lee
Steinhauer,
Dennis L.
Barton,
David C.
Taylor,
Brock
Chatson, and
Jitao
Zou*
Plant Biotechnology Institute, National Research Council of Canada,
110 Gymnasium Place, Saskatoon, SK S7N OW9, Canada
An Arabidopsis cDNA
(AtPGMp) encoding the plastidic phosphoglucomutase (PGM)
predicted a 623-amino acid protein with an N-terminal sequence typical
of a plastid signal peptide. Expression of a recombinant protein in
Escherichia coli confirmed its enzyme activity. The
recombinant enzyme had an apparent Km value
of 98.5 µM and a Vmax of 4.48 µmol min 1 (mg protein)1. The Calvin cycle
intermediates fructose-1,6-bisphosphate and ribulose-1,5-bisphosphate
exerted an inhibitory effect on PGM activity, supporting its proposed
involvement in controlling photosynthetic carbon flow. A point mutation
was identified in the AtPGMp gene of the
Arabidopsis pgm-1 mutant. The mutation in the mutant
transcript generated a stop codon at about one third of the wild-type
open reading frame, and thus rendered the polypeptide nonfunctional. Storage lipid analysis of the pgm-1 mutant seeds showed
a 40% reduction in oil content compared with that of wild type. Our results indicate that plastidic PGM is an important factor affecting carbon flux in triacylglycerol accumulation in oilseed plants, most
likely through its essential role in starch synthesis.
1
This is National Research Council of Canada
publication no. 43,782.
*
Corresponding author; e-mail jzou{at}pbi.nrc.ca; fax 306-975-4839.
© 2000 American Society of Plant Physiologists
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