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성과
논문 (학술지)

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

저자, 논문 구분, 저자, 학술지명, ISSN, SCI(SCIE포함) 구분, 학술지 출판 일자, 볼륨, 페이지, 학술지 임팩트 팩터, 학술대회명, 학술대회 개최국, 키워드 항목으로 구성된 논문 상세조회를 제공하고 데이터가 없는 항목에 대해서는 출력
등록번호 - SCI 구분?
 ※구분 : SCI(SCIE포함), 비SCI
SCI
저자명 (주·공동저자) -;
논문구분 국외전문학술지 학술지명 Fungal Genetics and Biology
ISSN 1087-1845 학술지 출판일자 2021-11-03
학술지 볼륨번호 157 논문페이지 1 ~ 12
학술지 임팩트팩터 3.5 기여율 0 %
초록
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.
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