title: Protein kinase C is essential for viability of the rice blast fungus Magnaporthe oryzae.
abstract: Protein kinase C constitutes a family of serine-threonine kinases found in all eukaryotes and implicated in a wide range of cellular functions, including regulation of cell growth, cellular differentiation and immunity. Here, we present three independent lines of evidence which indicate that protein kinase C is essential for viability of Magnaporthe oryzae. First, all attempts to generate a target deletion of PKC1, the single copy protein kinase C-encoding gene, proved unsuccessful. Secondly, conditional gene silencing of PKC1 by RNA interference led to severely reduced growth of the fungus, which was reversed by targeted deletion of the Dicer2-encoding gene, MDL2. Finally, selective kinase inhibition of protein kinase C by targeted allelic replacement with an analogue-sensitive PKC1(AS) allele led to specific loss of fungal viability in the presence of the PP1 inhibitor. Global transcriptional profiling following selective PKC inhibition identified significant changes in gene expression associated with cell wall re-modelling, autophagy, signal transduction and secondary metabolism. When considered together, these results suggest protein kinase C is essential for growth and development of M. oryzae with extensive downstream targets in addition to the cell integrity pathway. Targeting protein kinase C signalling may therefore prove an effective means of controlling rice blast disease.
authors.affiliation: School of Biosciences, University of Exeter, Geoffrey Pope Building, Stocker Road, Exeter, EX4 4QD, UK.
authors.forename: Tina J
authors.initials: TJ
authors.lastname: Penn
authors.affiliation: School of Biosciences, University of Exeter, Geoffrey Pope Building, Stocker Road, Exeter, EX4 4QD, UK.
authors.forename: Mark E
authors.initials: ME
authors.lastname: Wood
authors.affiliation: School of Biosciences, University of Exeter, Geoffrey Pope Building, Stocker Road, Exeter, EX4 4QD, UK.
authors.forename: Darren M
authors.initials: DM
authors.lastname: Soanes
authors.affiliation: Biological Sciences, Syngenta, Jeallott's Hill International Research Centre, Bracknell, RG42 6EY, UK.
authors.forename: Michael
authors.initials: M
authors.lastname: Csukai
authors.affiliation: Biological Sciences, Syngenta, Jeallott's Hill International Research Centre, Bracknell, RG42 6EY, UK.
authors.forename: Andrew John
authors.initials: AJ
authors.lastname: Corran
authors.affiliation: School of Biosciences, University of Exeter, Geoffrey Pope Building, Stocker Road, Exeter, EX4 4QD, UK.
authors.forename: Nicholas J
authors.initials: NJ
authors.lastname: Talbot
mesh_terms: D000595:Amino Acid Sequence; D002470:Cell Survival / Q000502:physiology; D005656:Fungal Proteins / Q000037:antagonists & inhibitors / Q000378:metabolism*; D054884:Host-Pathogen Interactions; D020082:Magnaporthe / Q000201:enzymology*; D008969:Molecular Sequence Data; D012275:Oryza / Q000382:microbiology; D010935:Plant Diseases / Q000382:microbiology; D011493:Protein Kinase C / Q000037:antagonists & inhibitors / Q000378:metabolism*; D034622:RNA Interference; D015398:Signal Transduction
chemical_list: D005656:Fungal Proteins; D011493:Protein Kinase C