The FtsHi Enzymes of Arabidopsis thaliana: Pseudo-Proteases with an Important Function.

The FtsHi Enzymes of Arabidopsis thaliana: Pseudo-Proteases with an Important Function.
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拟南芥的FTSHI酶:具有重要功能的伪蛋白酶。

DOI:
10.3390/ijms22115917
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发表时间:
2021-05-31
影响因子:
5.6
通讯作者:
Funk C
Funk C
中科院分区:
生物学2区
文献类型:
--
作者:
Mishra LS;Funk C

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FtsH金属蛋白酶在真细菌、动物和植物中发现,它们在膜蛋白的维持和蛋白水解中起着重要作用。它们的位置仅限于内共生起源的细胞器、叶绿体和线粒体。在模式生物拟南芥(Arabidopsis thaliana)中,存在17种膜结合的FtsH蛋白酶,其含有AAA+(与各种细胞活性相关的ATP酶)和Zn 2+金属蛋白酶结构域。然而,在其中5个中,锌结合基序HEXXH要么突变(FtsHi 1,2,4,5)或完全缺失(FtsHi 3),使这些酶推测在蛋白水解中无活性。尽管如此,假蛋白酶FtsHi 1,2,4,5的纯合无效突变体是胚胎致死的。纯合的FTSHi3或FTSHi1中的弱点突变体在整个植物生长和发育中受到影响。这篇综述将集中在有关FtsHi假蛋白酶及其参与蛋白质进口的研究结果,导致胚胎发生,种子生长,叶绿体,叶片发育和氧化应激管理的后果。
FtsH metalloproteases found in eubacteria, animals, and plants are well-known for their vital role in the maintenance and proteolysis of membrane proteins. Their location is restricted to organelles of endosymbiotic origin, the chloroplasts, and mitochondria. In the model organism Arabidopsis thaliana, there are 17 membrane-bound FtsH proteases containing an AAA+ (ATPase associated with various cellular activities) and a Zn2+ metalloprotease domain. However, in five of those, the zinc-binding motif HEXXH is either mutated (FtsHi1, 2, 4, 5) or completely missing (FtsHi3), rendering these enzymes presumably inactive in proteolysis. Still, homozygous null mutants of the pseudo-proteases FtsHi1, 2, 4, 5 are embryo-lethal. Homozygous ftshi3 or a weak point mutant in FTSHi1 are affected in overall plant growth and development. This review will focus on the findings concerning the FtsHi pseudo-proteases and their involvement in protein import, leading to consequences in embryogenesis, seed growth, chloroplast, and leaf development and oxidative stress management.
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