Karyopherin MoKap119-mediated nuclear import of cyclin-dependent kinase regulator MoCks1 is essential for Magnaporthe oryzae pathogenicity.
Shulin ZhangChaoxiang LinTian ZhouLian-Hui ZhangYi Zhen DengPublished in: Cellular microbiology (2019)
Nuclear import of proteins relies on nuclear import receptors called importins/karyopherins (Kaps), whose functions were reported in yeasts, fungi, plants, and animal cells, including cell cycle control, morphogenesis, stress sensing/response, and also fungal pathogenecity. However, limited is known about the physiological function and regulatory mechanism of protein import in the rice-blast fungus Magnaporthe oryzae. Here, we identified an ortholog of β-importin in M. oryzae encoded by an ortholog of KAP119 gene. Functional characterisation of this gene via reverse genetics revealed that it is required for vegetative growth, conidiation, melanin pigmentation, and pathogenicity of M. oryzae. The mokap119Δ mutant was also defective in formation of appressorium-like structure from hyphal tips. By affinity assay and liquid chromatography-tandem mass spectrometry, we identified potential MoKap119-interacting proteins and further verified that MoKap119 interacts with the cyclin-dependent kinase subunit MoCks1 and mediates its nuclear import. Transcriptional profiling indicated that MoKap119 may regulate transcription of infection-related genes via MoCks1 regulation of MoSom1. Overall, our findings provide a novel insight into the regulatory mechanism of M. oryzae pathogenesis likely by MoKap119-mediated nuclear import of the cyclin-dependent kinase subunit MoCks1.
Keyphrases
- cell cycle
- protein kinase
- liquid chromatography tandem mass spectrometry
- transcription factor
- cell proliferation
- cell cycle arrest
- genome wide
- tyrosine kinase
- single cell
- gene expression
- copy number
- candida albicans
- biofilm formation
- risk assessment
- oxidative stress
- small molecule
- pi k akt
- solid phase extraction
- climate change
- signaling pathway
- saccharomyces cerevisiae
- heat shock
- capillary electrophoresis