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三种环状结构域过氧化物酶在昆虫病原真菌球孢白僵菌生命周期中的功能见解

Functional insights of three RING-finger peroxins in the life cycle of the insect pathogenic fungus Beauveria bassiana.

作者信息

Lei Jia-Hui, Sun Ting-Fei, Feng Ming-Guang, Ying Sheng-Hua

机构信息

Institute of Microbiology, College of Life Sciences, Zhejiang University, Hangzhou, 310058, China.

出版信息

Curr Genet. 2023 Dec;69(4-6):267-276. doi: 10.1007/s00294-023-01275-1. Epub 2023 Nov 1.

Abstract

Peroxisomes play important roles in fungal physiological processes. The RING-finger complex consists of peroxins Pex2, Pex10, and Pex12 and is essential for recycling of receptors responsible for peroxisomal targeting of matrix proteins. In this study, these three peroxins were functionally characterized in the entomopathogenic fungus Beauveria bassiana (Bb). These three peroxins are associated with peroxisomes, in which BbPex2 interacted with BbPex10 and BbPex12. Ablation of these peroxins did not completely block the peroxisome biogenesis, but abolish peroxisomal targeting of matrix proteins via both PTS1 and PTS2 pathways. Three disruptants displayed different phenotypic defects in growth on nutrients and under stress conditions, but have similar defects in acetyl-CoA biosynthesis, development, and virulence. Strikingly, BbPex10 played a less important role in fungal growth on tested nutrients than other two peroxins; whereas, BbPex2 performed a less important contribution to fungal growth under stresses. This investigation reinforces the peroxisomal roles in the lifecycle of entomopathogenic fungi and highlights the unequal functions of different peroxins in peroxisomal biology.

摘要

过氧化物酶体在真菌生理过程中发挥着重要作用。泛素连接酶复合体由过氧化物酶Pex2、Pex10和Pex12组成,对于负责基质蛋白过氧化物酶体靶向的受体的循环利用至关重要。在本研究中,对昆虫病原真菌球孢白僵菌(Bb)中的这三种过氧化物酶进行了功能表征。这三种过氧化物酶与过氧化物酶体相关,其中BbPex2与BbPex10和BbPex12相互作用。缺失这些过氧化物酶并没有完全阻断过氧化物酶体的生物发生,但通过PTS1和PTS2途径消除了基质蛋白的过氧化物酶体靶向。三个突变体在营养生长和应激条件下表现出不同的表型缺陷,但在乙酰辅酶A生物合成、发育和毒力方面具有相似的缺陷。引人注目的是,BbPex10在测试营养物质上对真菌生长的作用比其他两种过氧化物酶小;而BbPex2在应激条件下对真菌生长的贡献较小。这项研究强化了过氧化物酶体在昆虫病原真菌生命周期中的作用,并突出了不同过氧化物酶在过氧化物酶体生物学中的不平等功能。

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