Abstract
Many functions of vacuole depend on the activity of vacuolar ATPase which is essential to maintain an acidic lumen and create the driving forces for massive fluxes of ions and metabolites through vacuolar membrane. In filamentous fungus Magnaporthe oryzae , subcellular colocalization and quinacrine staining suggested that the V1V0 domains of V-ATPase were fully assembled and the vacuoles were kept acidic during infection-related developments. Targeted gene disruption of MoVMA11 gene, encoding the putative c’ subunit of V-ATPase, impaired vacuolar acidification and mimicked the phenotypes of yeast V-ATPase mutants in the poor colony morphology, abolished asexual and sexual reproductions, selective carbon source utilization, and increased calcium and heavy metals sensitivities, however, not in the typical pH conditional lethality. Strikingly, aerial hyphae of the MoVMA11 null mutant intertwined with each other to form extremely thick filamentous structures. The results also implicated that MoVMA11 was involved in cell wall integrity and appressorium formation. Abundant non-melanized swollen structures and rare, small appressoria without penetration ability were produced at the hyphal tips of the ΔMovma11 mutant on onion epidermal cells. Finally, the MoVMA11 null mutant lost pathogenicity on both intact and wounded host leaves. Overall, our data indicated that MoVMA11, like other fungal VMA genes, is associated with numerous cellular functions and highlighted that V-ATPase is essential for infection-related morphogenesis and pathogenesis in M . oryzae .
Highlights
Vacuolar H+-ATPases (V-ATPases) are multisubunit enzymes composed of a peripheral ATPase sector (V1) and a membrane-bound proton-translocating sector (V0) [1,2]
Using protein sequences of S. cerevisiae V-ATPase subunits for BLASTP searches, we identified the repertoire of V-ATPase encoding genes in the M. oryzae genome
Eukaryotic V-ATPase is associated with numerous cellular functions [8], and the virulence of human pathogenic fungi, C. albicans and Cryptococcus neoformans, requires functional V-ATPase [13,52]
Summary
Vacuolar H+-ATPases (V-ATPases) are multisubunit enzymes composed of a peripheral ATPase sector (V1) and a membrane-bound proton-translocating sector (V0) [1,2]. Yeast V1 sector includes eight different subunits, designated A-H, whereas the V0 sector is comprised of subunit a, d, e, and the proteolipid c ring, which contains subunit c (vma3), c’ (vma11), and c′′ (vma). In higher eukaryotic cells, subunit c’ is absent from the proteolipid ring, which is composed of five c copies and a single c′′ subunit instead [5,7]. With the aid of dedicated assembly factors, yeast V0 sector is assembled in endoplasmic reticulum (ER) independently (or coordinately with V1 subunits) prior to trafficking to Golgi apparatus for the full assembly of V-ATPase holoenzymes [7,8]. Apart from Golgiderived secretory vesicles, eukaryotic V-ATPases reside and function on other intracellular compartments, including lysosomes/lysosome-like vacuoles, early and late endosomes [8,9]
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