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21 January 2010
Article (Scientific journals)
A Temperature-sensitive mutation in the Arabidopsis thaliana phosphomannomutase gene disrupts protein glycosylation and triggers cell death.
Hoeberichts, Frank A; Vaeck, Elke; Kiddle, Guy et al.
2008 • In Journal of Biological Chemistry, 283 (9), p. 5708-18
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Keywords :
Arabidopsis/enzymology/genetics; Ascorbic Acid/biosynthesis/genetics; Catalysis; Cell Death/genetics; Glycoproteins/biosynthesis/genetics; Glycosylation; Guanosine Diphosphate Mannose/biosynthesis/genetics; Hot Temperature; Mannosephosphates/biosynthesis/genetics; Mutation; Phenotype; Phosphotransferases (Phosphomutases)/genetics/metabolism; Plant Proteins/genetics/metabolism; Protein Disulfide-Isomerases/genetics/metabolism; Recombinant Proteins/genetics/metabolism; Seedling/enzymology/genetics
Abstract :
[en] Eukaryotic phosphomannomutases (PMMs) catalyze the interconversion of mannose 6-phosphate to mannose 1-phosphate and are essential to the biosynthesis of GDP-mannose. As such, plant PMMs are involved in ascorbic acid (AsA) biosynthesis and N-glycosylation. We report on the conditional phenotype of the temperature-sensitive Arabidopsis thaliana pmm-12 mutant. Mutant seedlings were phenotypically similar to wild type seedlings when grown at 16-18 degrees C but died within several days after transfer to 28 degrees C. This phenotype was observed throughout both vegetative and reproductive development. Protein extracts derived from pmm-12 plants had lower PMM protein and enzyme activity levels. In vitro biochemical analysis of recombinant proteins showed that the mutant PMM protein was compromised in its catalytic efficiency (K cat/K m). Despite significantly decreased AsA levels in pmm-12 plants, AsA deficiency could not account for the observed phenotype. Since, at restrictive temperature, total glycoprotein patterns were altered and glycosylation of protein-disulfide isomerase was perturbed, we propose that a deficiency in protein glycosylation is responsible for the observed cell death phenotype.
Disciplines :
Phytobiology (plant sciences, forestry, mycology...)
Author, co-author :
Hoeberichts, Frank A;  Flanders Institute for Biotechnology (VIB) > Department of Plant Systems Biology
Vaeck, Elke;  Flanders Institute for Biotechnology - VIB > Departement of Plant Systems Biology
Kiddle, Guy;  Rothamsted Research > Crop Performance and Improvement Division
Coppens, Emmy;  Flanders Institute for Biotechnology (VIB) > Department of Plant Systems Biology
van de Cotte, Brigitte;  Flanders Institute for Biotechnology (VIB) > Department of Plant Systems Biology
Adamantidis, Antoine ;  Université de Liège - ULiège > Département des sciences biomédicales et précliniques > Biochimie et physiologie humaine et pathologique
Ormenese, Sandra ;  Université de Liège - ULiège > Département des sciences de la vie > Physiologie végétale > Physiologie végétale
Foyer, Christine H;  Rothamsted Research > Crop Performance and Improvement Division
Zabeau, Marc;  Flanders Institute for Biotechnology (VIB) > Department of Plant Systems Biology
Inze, Dirk;  Flanders Institute for Biotechnology (VIB) > Department of Plant Systems Biology
Périlleux, Claire ;  Université de Liège - ULiège > Département des sciences de la vie > Physiologie végétale
Van Breusegem, Frank;  Flanders Institute for Biotechnology (VIB) > Department of Plant Systems Biology
Vuylsteke, Marnik;  Flanders Institute for Biotechnology (VIB) > Department of Plant Systems Biology
More authors (3 more) Less
Language :
English
Title :
A Temperature-sensitive mutation in the Arabidopsis thaliana phosphomannomutase gene disrupts protein glycosylation and triggers cell death.
Publication date :
2008
Journal title :
Journal of Biological Chemistry
ISSN :
0021-9258
eISSN :
1083-351X
Publisher :
American Society for Biochemistry and Molecular Biology, Baltimore, United States - Maryland
Volume :
283
Issue :
9
Pages :
5708-18
Peer reviewed :
Peer Reviewed verified by ORBi
Funders :
BELSPO - SPP Politique scientifique - Service Public Fédéral de Programmation Politique scientifique
Research Fund of the Ghent University
Research Foundation-Flanders

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