Research

The disruption of a G alpha subunit sheds new light on the pathogenicity of Stagonospora nodorum on wheat


Reference:

Solomon, P. S., Tan, K. C., Sanchez, P., Cooper, R. M. and Oliver, R. P., 2004. The disruption of a G alpha subunit sheds new light on the pathogenicity of Stagonospora nodorum on wheat. Molecular Plant-Microbe Interactions, 17 (5), pp. 456-466.

Related documents:

This repository does not currently have the full-text of this item.
You may be able to access a copy if URLs are provided below.

Official URL:

http://dx.doi.org/10.1094/MPMI.2004.17.5.456

Abstract

Gna1, a gene encoding a Gα subunit, a key component of signal transduction pathways, has been cloned and characterized in the wheat pathogen Stagonospora nodorum. Analysis of Gna1 expression during infection revealed a slight decrease in transcript levels shortly after germination, after which levels steadily increased until sporulation. Inactivation of Gna1 had a pleiotropic effect on phenotype. The Gna1 mutants were less pathogenic, attributed to coinciding with a defect in direct penetration. Also, Gna1 mutants were unable to sporulate, showed an albino phenotype, and secreted one or more brown pigments into growth media. Analysis of growth medium identified tyrosine, phenylalanine, and dihydroxyphenylalanine (L-DOPA) were excreted by the gna1 strains but not by wild type. The presence of these compounds, and the insensitivity of melanization to tricyclazole suggest that S. nodorum synthesizes melanin via the L-DOPA pathway, the first fungal phytopathogen described to do so. Decreases in protease (and several other depolymerases) activities and sensitivity to osmotic stress were other phenotypes identified in the Gna1 mutants. Gna1 is the first signal transduction gene to be cloned and characterized from S. nodorum and its inactivation has uncovered several previously unknown facets of pathogenicity.

Details

Item Type Articles
CreatorsSolomon, P. S., Tan, K. C., Sanchez, P., Cooper, R. M. and Oliver, R. P.
DOI10.1094/MPMI.2004.17.5.456
DepartmentsFaculty of Science > Biology & Biochemistry
RefereedYes
StatusPublished
ID Code3908
Additional InformationID number: ISI:000221016700002

Export

Actions (login required)

View Item