The cyclin dependent kinase subunit Cks1 is required for infection-associated development of the rice blast fungus Magnaporthe oryzae

Yue, Xiaofeng, Que, Yawei, Deng, Shuzhen, Xu, Lin, Oses-Ruiz, Miriam, Talbot, Nicholas J. ORCID: https://orcid.org/0000-0001-6434-7757, Peng, Youliang and Wang, Zhengyi (2017) The cyclin dependent kinase subunit Cks1 is required for infection-associated development of the rice blast fungus Magnaporthe oryzae. Environmental Microbiology, 19 (10). pp. 3959-3981. ISSN 1462-2912

Full text not available from this repository. (Request a copy)

Abstract

Cell cycle regulation is pivotal for proper cell division and cellular differentiation in eukaryotic cells. The central regulators that govern eukaryotic cell cycle progression are cyclin-dependent kinases (CDKs) and their partners. Here, we report that Magnaporthe oryzae CKS1 encodes a cyclin-dependent kinase subunit, which plays a significant role in regulation of plant infection. We demonstrate that CKS1 is a functional homolog of CKS1/SUC1 and can physically interact with the CDK protein Cdc28, and Som1, a downstream regulator of the cyclic AMP-dependent Protein Kinase A pathway. CKS1 deletion mutants are severely impaired in hyphal growth, sexual reproduction, melanin pigmentation and conidiogenesis. Cks1 mutants are able to form appressoria from hyphal tips, but these are unable to re-polarize, and rice infection is impaired. CKS1 also affects chitin and glucan synthase activity during cell wall differentiation and fungal hydrophobin function. CKS1, therefore, encodes a conserved CDK-binding partner, essential for appressorium-mediated plant infection by the rice blast fungus.

Item Type: Article
Uncontrolled Keywords: cks protein,mediated plant infection,cell-cycle,fission yeast,schizosaccharomyces-pombe,saccharomyces-cerevisiae,appressorium formation,crystal-structure,aspergillus-nidulans,transcription factor
Faculty \ School: Faculty of Science > The Sainsbury Laboratory
Depositing User: LivePure Connector
Date Deposited: 20 Mar 2019 12:30
Last Modified: 22 Oct 2022 04:28
URI: https://ueaeprints.uea.ac.uk/id/eprint/70279
DOI: 10.1111/1462-2920.13796

Actions (login required)

View Item View Item