Abstract:
:The vacuolar H+-ATPases (V-ATPases) are conserved ATP-dependent proton pumps that acidify intracellular compartments in eukaryotic cells. The role of Cpvma1, a V-ATPase catalytic subunit A of Cryphonectria parasitica, was investigated by generating cpvma1-overexpressing and cpvma1-silenced strains. The mutant strains were evaluated for phenotypic characteristics, V-ATPase activity, response to elevated pH and Ca2+ in the medium, virulence on chestnut, and accumulation of hypovirus RNA in the cells. Compared with the wild-type strain, cpvma1-overexpressing strains showed no significant difference in phenotype; however, cpvma1-silenced strains exhibited a phenotype of reduced growth rate, lower level of sporulation, and a marked decrease in V-ATPase activity and virulence. In addition, silencing of cpvma1 increased sensitivity to elevated pH and Ca2+, implicating an important role for Cpvma1 in pH adaptation and Ca2+ homeostasis. Furthermore, silencing of cpvma1 resulted in significantly decreased accumulation of hypoviral RNA. Taken together, our results indicate that Cpvma1 plays an important role in the regulation of phenotypic traits and virulence and the accumulation of hypovirus RNA in C. parasitica.
journal_name
Phytopathologyjournal_title
Phytopathologyauthors
Li R,Bai S,He Y,Chen Q,Yao Y,Wang J,Chen Bdoi
10.1094/PHYTO-08-18-0289-Rsubject
Has Abstractpub_date
2019-08-01 00:00:00pages
1417-1424issue
8eissn
0031-949Xissn
1943-7684journal_volume
109pub_type
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