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Plant Cell Advance Online Publication
Published on November 4, 2005; 10.1105/tpc.105.036285

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Received July 18, 2005
Returned for revision September 20, 2005
Accepted October 12, 2005

Endoplasmic Reticulum Glucosidase II Is Required for Pathogenicity of Ustilago maydis

Jan Schirawski 1, Heidi U. Böhnert 2, Gero Steinberg 1, Karen Snetselaar 3, Lubica Adamikowa 1, and Regine Kahmann 4*

1 Max-Planck-Institut für Terrestrische Mikrobiologie, D-35043 Marburg, Germany
2 Institut für Genetik und Mikrobiolgie, D-80638 Munich, Germany
3 Department of Biology, Saint Joseph's University, Philadelphia, Pennsylvania 19131-1395
4 Max-Planck-Institut für Terrestrische Mikrobiologie, D-35043 Marburg, Germany; Institut für Genetik und Mikrobiolgie, D-80638 Munich, Germany

* To whom correspondence should be addressed. E-mail: kahmann{at}staff.uni-marburg.de.

We identified a nonpathogenic strain of Ustilago maydis by tagging mutagenesis. The affected gene, glucosidase1 (gas1), displays similarity to catalytic {alpha}-subunits of endoplasmic reticulum (ER) glucosidase II. We have shown that Gas1 localizes to the ER and complements the temperature-sensitive phenotype of a Saccharomyces cerevisiae mutant lacking ER glucosidase II. gas1 deletion mutants were normal in growth and mating but were more sensitive to calcofluor and tunicamycin. Mutant infection hyphae displayed significant alterations in the distribution of cell wall material and were able to form appressoria and penetrate the plant surface but arrested growth in the epidermal cell layer. Electron microscopy analysis revealed that the plant-fungal interface between mutant hyphae and the plant plasma membrane was altered compared with the interface of penetrating wild-type hyphae. This may indicate that gas1 mutants provoke a plant response.






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