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

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 (6PF2...

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Veröffentlicht in:Journal of experimental botany. - 1985. - 56(2005), 414 vom: 06. Apr., Seite 1129-42
1. Verfasser: Bourgis, Fabienne (VerfasserIn)
Weitere Verfasser: Botha, Fredrik C, Mani, Srikrishnan, Hiten, Fletcher N, Rigden, Daniel J, Verbruggen, Nathalie
Format: Aufsatz
Sprache:English
Veröffentlicht: 2005
Zugriff auf das übergeordnete Werk:Journal of experimental botany
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Arabidopsis Proteins Carbon Radioisotopes DNA Primers DNA, Complementary DNA, Plant Phosphofructokinases EC 2.7.1 - Phosphoglycerate Mutase EC 5.4.2.11
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100 1 |a Bourgis, Fabienne  |e verfasserin  |4 aut 
245 1 0 |a Characterization and functional investigation of an Arabidopsis cDNA encoding a homologue to the d-PGMase superfamily 
264 1 |c 2005 
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500 |a Date Revised 24.11.2016 
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520 |a 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-(14)C] 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 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 7 |a Arabidopsis Proteins  |2 NLM 
650 7 |a Carbon Radioisotopes  |2 NLM 
650 7 |a DNA Primers  |2 NLM 
650 7 |a DNA, Complementary  |2 NLM 
650 7 |a DNA, Plant  |2 NLM 
650 7 |a Phosphofructokinases  |2 NLM 
650 7 |a EC 2.7.1 -  |2 NLM 
650 7 |a Phosphoglycerate Mutase  |2 NLM 
650 7 |a EC 5.4.2.11  |2 NLM 
700 1 |a Botha, Fredrik C  |e verfasserin  |4 aut 
700 1 |a Mani, Srikrishnan  |e verfasserin  |4 aut 
700 1 |a Hiten, Fletcher N  |e verfasserin  |4 aut 
700 1 |a Rigden, Daniel J  |e verfasserin  |4 aut 
700 1 |a Verbruggen, Nathalie  |e verfasserin  |4 aut 
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