Plant cysteine oxidases control the oxygen-dependent branch of the N-end-rule pathway.

Plant cysteine oxidases control the oxygen-dependent branch of the N-end-rule pathway.
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DOI:
10.1038/ncomms4425
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发表时间:
2014-03-06
影响因子:
16.6
通讯作者:
Licausi, Francesco
Licausi, Francesco
中科院分区:
综合性期刊1区
文献类型:
--
作者:
Weits, Daan A.;Giuntoli, Beatrice;Kosmacz, Monika;Parlanti, Sandro;Hubberten, Hans-Michael;Riegler, Heike;Hoefgen, Rainer;Perata, Pierdomenico;van Dongen, Joost T.;Licausi, Francesco

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在植物和动物细胞中,氨基端半胱氨酸氧化通过n端规则途径的氧依赖分支控制选择性蛋白质水解。目前尚不清楚n端半胱氨酸是如何被特异性氧化的。在这里,我们发现植物半胱氨酸氧化酶(PCO)酶利用氧作为共底物氧化ERF-VII转录因子的倒数第二半胱氨酸,从而控制这些蛋白的寿命。因此,ERF-VII蛋白在缺氧条件下稳定并激活对低氧的分子反应,而厌氧基因的表达在空气中受到抑制。PCO家族成员本身是ERF-VII转录因子的靶标,根据缺氧条件的程度产生适应应激反应的反馈回路。我们的研究结果表明,PCOs在植物中充当氧气的传感器蛋白,并提供了n端规则途径的主动调节如何平衡植物对最佳生长和发育的胁迫反应的例子。植物的氧感知是通过n端规则途径介导的,在该途径中,ERF-VII转录因子的n端半胱氨酸残基被选择性氧化。Weits等人发现了负责这种修饰的半胱氨酸氧化酶,并表明它们的表达本身受到ERF-VII的调节。
In plant and animal cells, amino-terminal cysteine oxidation controls selective proteolysis via an oxygen-dependent branch of the N-end rule pathway. It remains unknown how the N-terminal cysteine is specifically oxidized. Here we identify plant cysteine oxidase (PCO) enzymes that oxidize the penultimate cysteine of ERF-VII transcription factors by using oxygen as a co-substrate, thereby controlling the lifetime of these proteins. Consequently, ERF-VII proteins are stabilized under hypoxia and activate the molecular response to low oxygen while the expression of anaerobic genes is repressed in air. Members of the PCO family are themselves targets of ERF-VII transcription factors, generating a feedback loop that adapts the stress response according to the extent of the hypoxic condition. Our results reveal that PCOs act as sensor proteins for oxygen in plants and provide an example of how proactive regulation of the N-end rule pathway balances stress response to optimal growth and development in plants. Oxygen sensing in plants is mediated by the N-end rule pathway, in which the N-terminal cysteine residue of ERF-VII transcription factors is selectively oxidised. Weits et al. identify cysteine oxidases responsible for this modification, and show that their expression is itself regulated by ERF-VII.
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