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JXB Advance Access originally published online on March 31, 2003
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Journal of Experimental Botany, Vol. 54, No. 386, pp. 1351-1360, May 1, 2003
© 2003 Oxford University Press

Molecular and biochemical characterization of cytosolic phosphoglucomutase in wheat endosperm (Triticum aestivum L. cv. Axona)

Received 26 August 2002; Accepted 12 February 2003

Emma J. Davies1, Ian J. Tetlow2, Caroline G. Bowsher1 and Michael J. Emes3,2

1 School of Biological Sciences, 3.614 Stopford Building, Oxford Road, University of Manchester, Manchester M13 9PT, UK
2 Department of Botany, College of Biological Sciences, University of Guelph, Guelph, Ontario, N1G 4C4, Canada

Abbreviations: ADH, alcohol dehydrogenase; ADPG, ADPglucose; AGPase, ADPglucose pyrophosphorylase; APPase, alkaline inorganic pyrophosphatase; cyt c oxidase, cytochrome c oxidase; dpa, days post-anthesis; Na2-EDTA, disodium ethylenediaminetetra-acetic acid; G1P, glucose 1-phosphate; G6P, glucose 6-phosphate; G16BP, glucose 1,6-bisphosphate; PGM, phosphoglucomutase; PMSF, phenyl methyl sulphonyl fluoride; UGPase, uridine 5' diphosphate glucose pyrophosphorylase.

Evidence from a number of plant tissues suggests that phosphoglucomutase (PGM) is present in both the cytosol and the plastid. The cytosolic and plastidic isoforms of PGM have been partially purified from wheat endosperm (Triticum aestivum L. cv. Axona). Both isoforms required glucose 1,6-bisphosphate for their activity with Ka values of 4.5 µM and 3.8 µM for cytosolic and plastidic isoforms, respectively, and followed normal Michaelis–Menten kinetics with glucose 1-phosphate as the substrate with Km values of 0.1 mM and 0.12 mM for the cytosolic and plastidic isoforms, respectively. A cDNA clone was isolated from wheat endosperm that encodes the cytosolic isoform of PGM. The deduced amino acid sequence shows significant homology to PGMs from eukaryotic and prokaryotic sources. PGM activity was measured in whole cell extracts and in amyloplasts isolated during the development of wheat endosperm. Results indicate an approximate 80% reduction in measurable activity of plastidial and cytosolic PGM between 8 d and 30 d post-anthesis. Northern analysis showed a reduction in cytosolic PGM mRNA accumulation during the same period of development. The implications of the changes in PGM activity during the synthesis of starch in developing endosperm are discussed.

Key words: Phosphoglucomutase, starch synthesis, Triticum aestivum.


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