Aberrant protein N- glycosylation impacts upon infection-related growth transitions of the haploid plant-pathogenic fungus Mycosphaerella graminicola

A - Papers appearing in refereed journals

Motteram, J., Lovegrove, A., Pirie, E. J., Marsh, J., Devonshire, J., Van De Meene, A., Hammond-Kosack, K. E. and Rudd, J. J. 2011. Aberrant protein N- glycosylation impacts upon infection-related growth transitions of the haploid plant-pathogenic fungus Mycosphaerella graminicola. Molecular MicroBiology. 81 (2), pp. 415-433.

AuthorsMotteram, J., Lovegrove, A., Pirie, E. J., Marsh, J., Devonshire, J., Van De Meene, A., Hammond-Kosack, K. E. and Rudd, J. J.
Abstract

The ascomycete fungus Mycosphaerella graminicola is the causal agent of Septoria Tritici Blotch disease of wheat and can grow as yeast-like cells or as hyphae depending on environmental conditions. Hyphal growth is however essential for successful leaf infection. A T-DNA mutagenesis screen performed on haploid spores identified a mutant, which can undergo yeast-like growth but cannot switch to hyphal growth. For this reason the mutant was non-pathogenic towards wheat leaves. The gene affected, MgAlg2, encoded a homologue of Saccharomyces cerevisiae ScAlg2, an alpha-1,2-mannosyltransferase, which functions in the early stages of asparagine-linked protein (N-) glycosylation. Targeted gene deletion and complementation experiments confirmed that loss of MgAlg2 function prevented the developmental growth switch. MgAlg2 was able to functionally complement the S. cerevisiae ScAlg2-1 temperature sensitive growth phenotype. Spores of Delta MgAlg2 mutants were hypersensitive to the cell wall disrupting agent Calcofluor white and produced abnormally hypo-N-glycosylated proteins. Gene expression, proteome and glycoproteome analysis revealed that Delta MgAlg2 mutant spores show responses typically associated with the accumulation of mis-folded proteins. The data presented highlight key roles for protein N-glycosylation in regulating the switch to hyphal growth, possibly as a consequence of maintaining correct folding and localization of key proteins involved in this process.

KeywordsBiochemistry & Molecular Biology; Microbiology
Year of Publication2011
JournalMolecular MicroBiology
Journal citation81 (2), pp. 415-433
Digital Object Identifier (DOI)doi:10.1111/j.1365-2958.2011.07701.x
PubMed ID21623954
Open accessPublished as green open access
FunderBiotechnology and Biological Sciences Research Council
Funder project or codeCentre for Sustainable Pest and Disease Management (PDM)
Publisher's version
ISSN0950382X
0950-382X
PublisherWiley

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