ORBi: Hoeberichts Frank A - A Temperature-sensitive mutation in the Arabidopsis thaliana phosphomannomutase gene disrupts protein glycosylation and triggers cell death.

Reference : A Temperature-sensitive mutation in the Arabidopsis thaliana phosphomannomutase gene dis...


	Document type :	Scientific journals : Article
	Discipline(s) :	Life sciences : Phytobiology (plant sciences, forestry, mycology...)
	To cite this reference:	http://hdl.handle.net/2268/11334

Title :	A Temperature-sensitive mutation in the Arabidopsis thaliana phosphomannomutase gene disrupts protein glycosylation and triggers cell death.
Language :	English
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 - ULg > Département des sciences biomédicales et précliniques > Biochimie et physiologie humaine et pathologique >]
	Ormenese, Sandra [Université de Liège - ULg > 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 - ULg > 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 > > > > > >]
Publication date :	2008
Journal title :	Journal of Biological Chemistry
Publisher :	American Society for Biochemistry and Molecular Biology
Volume :	283
Issue/season :	9
Pages :	5708-18
Peer reviewed :	Yes (verified by ORBi)
Audience :	International
ISSN :	0021-9258
e-ISSN :	1083-351X
City :	Baltimore
Country :	MD
Keywords :	[en] 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.
Funders :	Politique Scientifique Fédérale (Belgique) = Belgian Federal Science Policy ; Research Fund of the Ghent University ; Research Foundation-Flanders
Target :	Researchers
Permalink :	http://hdl.handle.net/2268/11334
DOI :	10.1074/jbc.M704991200

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