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Plant Physiol, February 2001, Vol. 125, pp. 818-827
A Cytosolic ADP-Glucose Pyrophosphorylase Is a Feature of
Graminaceous Endosperms, But Not of Other Starch-Storing
Organs1
Diane M.
Beckles,2
Alison M.
Smith,* and
Tom
ap
Rees3
Department of Plant Sciences, University of Cambridge, Downing
Street, Cambridge CB2 3EA, United Kingdom (D.M.B, T. a.R.); and
Department of Applied Genetics, John Innes Centre, Colney Lane, Norwich
NR4 7UH, United Kingdom (D.M.B., A.M.S.)
The occurrence of an extra-plastidial isoform of ADP-glucose (Glc)
pyrophosphorylase (AGPase) among starch-storing organs was investigated
in two ways. First, the possibility that an extra-plastidial isoform
arose during the domestication of cereals was studied by comparing the
intracellular distribution of enzyme activity and protein in developing
endosperm of noncultivated Hordeum species with that
previously reported for cultivated barley (Hordeum
vulgare). As in cultivated barley, the AGPase of H. vulgare subsp. spontaneum and Hordeum
murinum endosperm is accounted for by a major extra-plastidial and a minor plastidial isoform. Second, the ratio of ADP-Glc to UDP-Glc
was used as an indication of the intracellular location of the AGPase
activity in a wide range of starch-synthesizing organs. The ratio is
expected to be high in organs in which UDP-Glc and ADP-Glc are
synthesized primarily in the cytosol, because the reactions catalyzed
by AGPase and UDP-Glc pyrophosphorylase will be coupled and close to
equilibrium. This study revealed that ADP-Glc contents and the ratio of
ADP-Glc to UDP-Glc were higher in developing graminaceous endosperms
than in any other starch-storing organs. Taken as a whole the results
indicate that an extra-plastidial AGPase is important in ADP-Glc
synthesis in graminaceous endosperms, but not in other starch-storing
organs.
1
This work was supported by a Competitive
Strategic Grant from the Biotechnology and Biological Sciences Research
Council (UK) at the John Innes Centre. D.M.B. was supported by a
studentship from the Commonwealth Scholarship Commission.
2
Present address: DuPont Agricultural Products,
Experimental Station, P.O. Box 80402, Wilmington, DE
19880-0402.
3
Deceased. This work was started in Tom ap
Rees's laboratory prior to his death in 1996.
*
Corresponding author; e-mail alison.smith{at}bbsrc.ac.uk; fax
44-1603-450045.
© 2001 American Society of Plant Physiologists
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