Pex7 selectively imports PTS2 target proteins to peroxisomes and is required for anthracnose disease development in Colletotrichum scovillei.

Autor: Shin JH; Division of Bio-Resource Sciences, Bio-Herb Research Institute, and Interdisciplinary Program in Smart Agriculture, Kangwon National University, Chuncheon, Republic of Korea., Fu T; Division of Bio-Resource Sciences, Bio-Herb Research Institute, and Interdisciplinary Program in Smart Agriculture, Kangwon National University, Chuncheon, Republic of Korea., Kim KS; Division of Bio-Resource Sciences, Bio-Herb Research Institute, and Interdisciplinary Program in Smart Agriculture, Kangwon National University, Chuncheon, Republic of Korea. Electronic address: kims@kangwon.ac.kr.
Jazyk: angličtina
Zdroj: Fungal genetics and biology : FG & B [Fungal Genet Biol] 2021 Dec; Vol. 157, pp. 103636. Date of Electronic Publication: 2021 Nov 03.
DOI: 10.1016/j.fgb.2021.103636
Abstrakt: Pex7 is a shuttling receptor that imports matrix proteins with a type 2 peroxisomal targeting signal (PTS2) to peroxisomes. The Pex7-mediated PTS2 protein import contributes to crucial metabolic processes such as the fatty acid β-oxidation and glucose metabolism in a number of fungi, but cellular roles of Pex7 between the import of PTS2 target proteins and metabolic processes have not been fully understood. In this study, we investigated the functional roles of CsPex7, a homolog of the yeast Pex7, by targeted gene deletion in the pepper anthracnose fungus Colletotrichum scovillei. CsPex7 was required for carbon source utilization, scavenging of reactive oxygen species, conidial production, and disease development in C. scovillei. The expression of fluorescently tagged PTS2 signal of hexokinases and 3-ketoacyl-CoA thiolases showed that peroxisomal localization of the hexokinase CsGlk1 PTS2 is dependent on CsPex7, but those of the 3-ketoacyl-CoA thiolases are independent on CsPex7. In addition, GFP-tagged CsPex7 proteins were intensely localized to the peroxisomes on glucose-containing media, indicating a role of CsPex7 in glucose utilization. Collectively, these findings indicate that CsPex7 selectively recognizes specific PTS2 signal for import of PTS2-containing proteins to peroxisomes, thereby mediating peroxisomal targeting efficiency of PTS2-containing proteins in C. scovillei. On pepper fruits, the ΔCspex7 mutant exhibited significantly reduced virulence, in which excessive accumulation of hydrogen peroxide was observed in the pepper cells. We think the reduced virulence results from the abnormality in hydrogen peroxide metabolism of the ΔCspex7 mutant. Our findings provide insight into the cellular roles of CsPex7 in PTS2 protein import system.
(Copyright © 2021 Elsevier Inc. All rights reserved.)
Databáze: MEDLINE
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