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.
|Authors||Motteram, J., Lovegrove, A., Pirie, E. J., Marsh, J., Devonshire, J., Van De Meene, A., Hammond-Kosack, K. E. and Rudd, J. J.|
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.
|Keywords||Biochemistry & Molecular Biology; Microbiology|
|Year of Publication||2011|
|Journal citation||81 (2), pp. 415-433|
|Digital Object Identifier (DOI)||doi:10.1111/j.1365-2958.2011.07701.x|
|Open access||Published as green open access|
|Funder||Biotechnology and Biological Sciences Research Council|
|Funder project or code||Centre for Sustainable Pest and Disease Management (PDM)|
|A functional genomics approach to the identification of genes determining fungal pathogenesis of cereals|
|Pathogenicity of non-biotrophic fungi infecting cereals|
Permalink - https://repository.rothamsted.ac.uk/item/8q8y7/aberrant-protein-n-glycosylation-impacts-upon-infection-related-growth-transitions-of-the-haploid-plant-pathogenic-fungus-mycosphaerella-graminicola