A Deubiquitinating Enzyme Ubp14 Is Required for Development, Stress Response, Nutrient Utilization, and Pathogenesis of Magnaporthe oryzae.

摘要: Ubiquitination is an essential protein modification in eukaryotic cells, which reversible. Deubiquitinating enzymes (DUBs) catalyze deubiquitination process to reverse ubiquitination, maintain ubiquitin homeostasis or promote degradation by recycling ubiquitins. In order investigate effects of plant pathogenic fungus Magnaporthe oryzae, we generated deletion mutants MoUBP14. Ortholog MoUbp14 was reported play general roles ubiquitin-mediated Saccharomyces cerevisiae. The ΔMoubp14 mutant lost its pathogenicity and severely reduced mycelial growth, sporulation, carbon source utilization, increased sensitivity distinct stresses. blocked penetration, could due defect turgor generation. It also invasive reduction stress tolerance nutrient utilization. Deletion UBP14 led accumulation free polyubiquitin chains. Pulldown assay identified some proteins related carbohydrate metabolism response may putatively interact with MoUbp14, including two key rate-limiting gluconeogenesis, MoFbp1 MoPck1. These were degraded when the glucose supplied M. oryzae grown low media for a short period time (∼12 h), this required MoUbp14. summary, pleiotropic phenotypes indicated that different developments oryzae.