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A temperature-sensitive mutation in the Arabidopsis thaliana phosphomannomutase gene disrupts protein glycosylation and triggers cell death

Lookup NU author(s): Professor Christine Foyer


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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 °C but died within several days after transfer to 28 °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/Km). 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. © 2008 by The American Society for Biochemistry and Molecular Biology, Inc.

Publication metadata

Author(s): Hoeberichts FA, Vaeck E, Kiddle G, Coppens E, Van De Cotte B, Adamantidis A, Ormenese S, Foyer CH, Zabeau M, Inze D, Perilleux C, Van Breusegem F, Vuylsteke M

Publication type: Article

Publication status: Published

Journal: Journal of Biological Chemistry

Year: 2008

Volume: 283

Issue: 9

Pages: 5708-5718

ISSN (print): 0021-9258

ISSN (electronic): 1083-351X

Publisher: American Society for Biochemistry and Molecular Biology, Inc.


DOI: 10.1074/jbc.M704991200

PubMed id: 18086684


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