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JXB Advance Access originally published online on February 28, 2005
Journal of Experimental Botany 2005 56(414):1129-1142; doi:10.1093/jxb/eri105
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© The Author [2005]. Published by Oxford University Press [on behalf of the Society for Experimental Biology]. All rights reserved. For Permissions, please e-mail: journals.permissions@oupjournals.org

RESEARCH PAPER

Characterization and functional investigation of an Arabidopsis cDNA encoding a homologue to the d-PGMase superfamily

Fabienne Bourgis1,2 *, Fredrik C. Botha3 {dagger}, Srikrishnan Mani2 {ddagger}, Fletcher N. Hiten3, Daniel J. Rigden4 and Nathalie Verbruggen1,2,§

1Laboratoire de Physiologie et de Génétique Moléculaire des Plantes, Université Libre de Bruxelles, CP 242, Bd du Triomphe, B-1050 Bruxelles, Belgium
2Vakgroep Moleculaire Genetica and Department of Plant Systems Biology, Vlaams Interuniversitair Instituut voor Biotechnologie (VIB), Universiteit Gent, Technologiepark 927, B-9052 Gent, Belgium
3Institute for Plant Biotechnology, University of Stellenbosch, Private Bag, 7602 Matieland, South Africa
4National Centre of Genetic Resources and Biotechnology, Cenargen/Embrapa, S.A.I.N. Parque Rural, Final W3, Asa Norte, 70770-900 Brasilia, Brazil

§ To whom correspondence should be addressed. Fax: +32 2 650 5421. E-mail: nverbru{at}ulb.ac.be

An Arabidopsis thaliana cDNA (At-74) has been isolated that encoded an uncharacterized protein showing homology with members of the d-PGMase superfamily: cofactor-dependent phosphoglycerate mutases (d-PGM-ases) and the phosphatase domain of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatases (6PF2Kase/F2, 6Pase). Preliminary phylogenetic studies indicated that At-74 cDNA and its close homologue in Arabidopsis, At-74H, belong, however, to an equally distinct group. At-74 was ubiquitously expressed in vegetative organs and induced by glucose. The At-74 cDNA was overexpressed in A. thaliana to investigate its function, but this overexpression did not result in a clear phenotype. Enzymatic assays performed on At-74-overproducing transgenic plants or E. coli cells showed no increase in either the activities of cofactor-dependent and -independent phosphoglycerate mutases (i-PGMases) and F2,6Pase or that of acid phosphatases. The possible role of At-74 in plant metabolism was further investigated by carbon partitioning experiments with [U-14C] glucose and measurements of soluble sugars in both young leaves and roots. Two overexpressing At-74 lines showed a clear increase in glucose uptake. This paper introduces the At-74 homologue of the d-PGMase superfamily members and supports a possible role of At-74 in carbohydrate metabolism.

Key words: d-PGMase family, transgenic plants, [U-14C]glucose feeding


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