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

Functional insights of three RING-finger peroxins in the life cycle of the insect pathogenic fungus Beauveria bassiana
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DOI:
10.1007/s00294-023-01275-1
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发表时间:
2023-11
期刊:
影响因子:
2.5
通讯作者:
J. Lei;Ting-Fei Sun;M. Feng;S. Ying
J. Lei;Ting-Fei Sun;M. Feng;S. Ying
中科院分区:
生物学3区
文献类型:
--
作者:
J. Lei;Ting-Fei Sun;M. Feng;S. Ying

文献摘要

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过氧化物酶体在真菌生理过程中发挥重要作用。 RING-finger 复合物由过氧化物蛋白 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回收至关重要。在本研究中,这三种过氧化物酶在昆虫病原真菌白僵菌(Bb)中进行了功能表征。这三种过氧化物素与过氧化物酶体相关,其中 BbPex2 与 BbPex10 和 BbPex12 相互作用。这些过氧化物酶的消除并没有完全阻断过氧化物酶体的生物发生,但消除了通过 PTS1 和 PTS2 途径对基质蛋白的过氧化物酶体靶向。三种破坏株在营养物质和胁迫条件下的生长中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,与其他两种过氧化物酶相比,BbPex10 在测试营养素的真菌生长中发挥的作用不太重要。然而,BbPex2 在压力下对真菌生长的贡献不太重要。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,并强调了不同过氧化物酶在过氧化物酶体生物学中的不同功能。
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 fungusBeauveria 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.