title: Proteins interacting with mitochondrial ATP-dependent Lon protease (MAP1) in Magnaporthe oryzae are involved in rice blast disease.
abstract: The ATP-dependent Lon protease is involved in many physiological processes. In bacteria, Lon regulates pathogenesis and, in yeast, Lon protects mitochondia from oxidative damage. However, little is known about Lon in fungal phytopathogens. MAP1, a homologue of Lon in Magnaporthe oryzae, was recently identified to be important for stress resistance and pathogenesis. Here, we focus on a novel pathogenic pathway mediated by MAP1. Based on an interaction system between rice and a tandem affinity purification (TAP)-tagged MAP1 complementation strain, we identified 23 novel fungal proteins from infected leaves using a TAP approach with mass spectrometry, and confirmed that 14 of these proteins physically interact with MAP1 in vivo. Among these 14 proteins, 11 candidates, presumably localized to the mitochondria, were biochemically determined to be substrates of MAP1 hydrolysis. Deletion mutants were created and functionally analysed to further confirm the involvement of these proteins in pathogenesis. The results indicated that all mutants showed reduced conidiation and sensitivity to hydrogen peroxide. Appressorial formations were not affected, although conidia from certain mutants were morphologically altered. In addition, virulence was reduced in four mutants, enhanced (with lesions forming earlier) in two mutants and remained unchanged in one mutant. Together with the known virulence-related proteins alternative oxidase and enoyl-CoA hydratase, we propose that most of the Lon-interacting proteins are involved in the pathogenic regulation pathway mediated by MAP1 in M. oryzae. Perturbation of this pathway may represent an effective approach for the inhibition of rice blast disease.
authors.affiliation: College of Plant Sciences, Jilin University, Changchun, 130062, China.
authors.forename: Xiao
authors.initials: X
authors.lastname: Cui
authors.affiliation: College of Plant Sciences, Jilin University, Changchun, 130062, China.
authors.forename: Yi
authors.initials: Y
authors.lastname: Wei
authors.affiliation: College of Plant Sciences, Jilin University, Changchun, 130062, China.
authors.forename: Yu-Han
authors.initials: YH
authors.lastname: Wang
authors.affiliation: College of Plant Sciences, Jilin University, Changchun, 130062, China.
authors.forename: Jian
authors.initials: J
authors.lastname: Li
authors.affiliation: Department of Biology, The Chinese University of Hong Kong, 999077, Hong Kong SAR.
authors.forename: Fuk-Ling
authors.initials: FL
authors.lastname: Wong
authors.affiliation: College of Plant Sciences, Jilin University, Changchun, 130062, China.
authors.forename: Ya-Jie
authors.initials: YJ
authors.lastname: Zheng
authors.affiliation: College of Plant Sciences, Jilin University, Changchun, 130062, China.
authors.forename: Hai
authors.initials: H
authors.lastname: Yan
authors.affiliation: College of Plant Sciences, Jilin University, Changchun, 130062, China.
authors.forename: Shao-Shuai
authors.initials: SS
authors.lastname: Liu
authors.affiliation: College of Plant Sciences, Jilin University, Changchun, 130062, China.
authors.forename: Jin-Liang
authors.initials: JL
authors.lastname: Liu
authors.affiliation: College of Plant Sciences, Jilin University, Changchun, 130062, China.
authors.forename: Bao-Lei
authors.initials: BL
authors.lastname: Jia
authors.affiliation: College of Plant Sciences, Jilin University, Changchun, 130062, China.
authors.forename: Shi-Hong
authors.initials: SH
authors.lastname: Zhang
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism*; D002846:Chromatography, Affinity; D020082:Magnaporthe / Q000201:enzymology*; D008928:Mitochondria / Q000201:enzymology*; D008969:Molecular Sequence Data; D009181:Mycoses / Q000201:enzymology / Q000378:metabolism*; D012275:Oryza / Q000382:microbiology*; D049070:Protease La / Q000302:isolation & purification / Q000378:metabolism*
chemical_list: D000255:Adenosine Triphosphate; D049070:Protease La
keywords: Magnaporthe oryzae; interacting proteins; mitochondrial ATP-dependent Lon protease