Journal
MOLECULAR MICROBIOLOGY
Volume 81, Issue 2, Pages 415-433Publisher
WILEY-BLACKWELL
DOI: 10.1111/j.1365-2958.2011.07701.x
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Funding
- Biotechnology and Biological Sciences Research Council (BBSRC) of the UK
- Biotechnology and Biological Sciences Research Council [BBS/E/C/00004973, BBS/E/C/00004972] Funding Source: researchfish
- BBSRC [BBS/E/C/00004972, BBS/E/C/00004973] Funding Source: UKRI
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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.
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