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pex13 和 pex14 是过氧化物酶体对接复合物的关键组成部分,对于稻瘟病菌过氧化物酶体的形成、宿主感染和与致病性相关的形态发生是必需的。

Pex13 and Pex14, the key components of the peroxisomal docking complex, are required for peroxisome formation, host infection and pathogenicity-related morphogenesis in Magnaporthe oryzae.

机构信息

a State Key Laboratory Breeding Base for Zhejiang Sustainable Pest and Disease Control, Institute of Plant Protection Microbiology , Zhejiang Academy of Agricultural Sciences , Hangzhou , China.

b The Key Laboratory for Quality Improvement of Agricultural Products of Zhejiang Province, School of Agricultural and Food Sciences , Zhejiang Agriculture and Forest University , Hangzhou , China.

出版信息

Virulence. 2019 Dec;10(1):292-314. doi: 10.1080/21505594.2019.1598172.

DOI:10.1080/21505594.2019.1598172
PMID:30905264
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC6527019/
Abstract

Peroxisomes are ubiquitous organelles in eukaryotic cells that fulfill multiple important metabolisms. Pex13 and Pex14 are key components of the peroxisomal docking complex in yeasts and mammals. In the present work, we functionally characterized the homologues of Pex13 and Pex14 (Mopex13 and Mopex14) in the rice blast fungus Magnaporthe oryzae. Mopex13 and Mopex14 were peroxisomal membrane distributed and were both essential for the maintenance of Mopex14/17 on the peroxisomal membrane. Mopex13 and Mopex14 interacted with each other, and with Mopex14/17 and peroxisomal matrix protein receptors. Disruption of Mopex13 and Mopex14 resulted in a cytoplasmic distribution of peroxisomal matrix proteins and the Woronin body protein Hex1. In the ultrastructure of Δmopex13 and Δmopex14 cells, peroxisomes were detected on fewer occasions, and the Woronin bodies and related structures were dramatically affected. The Δmopex13 and Δmopex14 mutants were reduced in vegetative growth, conidial generation and mycelial melanization, in addition, Δmopex13 showed reduced conidial germination and appressorial formation and abnomal appressorial morphology. Both Δmopex13 and Δmopex14 were deficient in appressorial turgor and nonpathogenic to their hosts. The infection failures in Δmopex13 and Δmopex14 were also due to their reduced ability to degrade fatty acids and to endure reactive oxygen species and cell wall-disrupting compounds. Additionally, Mopex13 and Mopex14 were required for the sexual reproduction of the fungus. These data indicate that Mopex13 and Mopex14, as key components of the peroxisomal docking complex, are indispensable for peroxisomal biogenesis, fungal development and pathogenicity in the rice blast fungus.

摘要

过氧化物酶体是真核细胞中普遍存在的细胞器,它们完成多种重要的代谢过程。Pex13 和 Pex14 是酵母和哺乳动物过氧化物酶体对接复合物的关键组成部分。在本工作中,我们对水稻稻瘟病菌中的 Pex13 和 Pex14(Mopex13 和 Mopex14)同源物进行了功能表征。Mopex13 和 Mopex14 定位于过氧化物酶体膜,对于 Mopex14/17 在过氧化物酶体膜上的维持都是必需的。Mopex13 和 Mopex14 相互作用,与 Mopex14/17 和过氧化物酶体基质蛋白受体相互作用。Mopex13 和 Mopex14 的缺失导致过氧化物酶体基质蛋白和沃罗宁体蛋白 Hex1 的细胞质分布。在Δmopex13 和Δmopex14 细胞的超微结构中,过氧化物酶体的出现频率降低,沃罗宁体和相关结构受到显著影响。Δmopex13 和Δmopex14 突变体在营养生长、分生孢子生成和菌丝体黑化方面受到抑制,此外,Δmopex13 的分生孢子萌发和附着胞形成以及附着胞形态异常受到抑制。Δmopex13 和Δmopex14 均缺乏附着胞膨压,对其宿主无致病性。Δmopex13 和Δmopex14 的感染失败也是由于它们降低了降解脂肪酸以及耐受活性氧和破坏细胞壁化合物的能力。此外,Mopex13 和 Mopex14 还需要真菌的有性生殖。这些数据表明,Mopex13 和 Mopex14 作为过氧化物酶体对接复合物的关键组成部分,对于过氧化物酶体的生物发生、真菌的发育和致病性是不可或缺的。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0359/6527019/bbb07f20382f/kvir-10-01-1598172-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0359/6527019/0831282e4c07/kvir-10-01-1598172-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0359/6527019/090744c0c787/kvir-10-01-1598172-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0359/6527019/36b5c6e298a4/kvir-10-01-1598172-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0359/6527019/65d9f4d28943/kvir-10-01-1598172-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0359/6527019/69093331738e/kvir-10-01-1598172-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0359/6527019/ac6d01ce50ca/kvir-10-01-1598172-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0359/6527019/bbb07f20382f/kvir-10-01-1598172-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0359/6527019/0831282e4c07/kvir-10-01-1598172-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0359/6527019/090744c0c787/kvir-10-01-1598172-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0359/6527019/36b5c6e298a4/kvir-10-01-1598172-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0359/6527019/65d9f4d28943/kvir-10-01-1598172-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0359/6527019/69093331738e/kvir-10-01-1598172-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0359/6527019/ac6d01ce50ca/kvir-10-01-1598172-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0359/6527019/bbb07f20382f/kvir-10-01-1598172-g007.jpg

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