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铁调素与 BRUTUS 相互作用以维持. 中的铁稳态。

IRON MAN interacts with BRUTUS to maintain iron homeostasis in .

机构信息

CAS Key Laboratory of Tropical Plant Resources and Sustainable Use, Xishuangbanna Tropical Botanical Garden, The Innovative Academy of Seed Design, Chinese Academy of Sciences, Kunming, Yunnan 650223, China.

Center of Economic Botany, Core Botanical Gardens, Chinese Academy of Sciences, Mengla 666303, China.

出版信息

Proc Natl Acad Sci U S A. 2021 Sep 28;118(39). doi: 10.1073/pnas.2109063118.

Abstract

IRON MAN (IMA) peptides, a family of small peptides, control iron (Fe) transport in plants, but their roles in Fe signaling remain unclear. BRUTUS (BTS) is a potential Fe sensor that negatively regulates Fe homeostasis by promoting the ubiquitin-mediated degradation of bHLH105 and bHLH115, two positive regulators of the Fe deficiency response. Here, we show that IMA peptides interact with BTS. The C-terminal parts of IMA peptides contain a conserved BTS interaction domain (BID) that is responsible for their interaction with the C terminus of BTS. plants constitutively expressing genes phenocopy the mutant. Moreover, IMA peptides are ubiquitinated and degraded by BTS. bHLH105 and bHLH115 also share a BID, which accounts for their interaction with BTS. IMA peptides compete with bHLH105/bHLH115 for interaction with BTS, thereby inhibiting the degradation of these transcription factors by BTS. Genetic analyses suggest that bHLH105/bHLH115 and IMA3 have additive roles and function downstream of BTS. Moreover, the transcription of both and is activated directly by bHLH105 and bHLH115 under Fe-deficient conditions. Our findings provide a conceptual framework for understanding the regulation of Fe homeostasis: IMA peptides protect bHLH105/bHLH115 from degradation by sequestering BTS, thereby activating the Fe deficiency response.

摘要

铁调控肽(IMA)是一类小肽,它们在植物中铁(Fe)的运输中起作用,但它们在 Fe 信号中的作用尚不清楚。BRUTUS(BTS)是一种潜在的 Fe 感受器,通过促进 bHLH105 和 bHLH115 的泛素介导的降解,负调控 Fe 稳态,bHLH105 和 bHLH115 是 Fe 缺乏反应的两个正调控因子。在这里,我们表明 IMA 肽与 BTS 相互作用。IMA 肽的 C 末端包含一个保守的 BTS 相互作用结构域(BID),负责其与 BTS C 末端的相互作用。组成型表达 基因的 植物表现出 突变体的表型。此外,IMA 肽被 BTS 泛素化和降解。bHLH105 和 bHLH115 也共享一个 BID,这解释了它们与 BTS 的相互作用。IMA 肽与 bHLH105/bHLH115 竞争与 BTS 的相互作用,从而抑制这些转录因子被 BTS 降解。遗传分析表明,bHLH105/bHLH115 和 IMA3 具有累加作用,并在 BTS 下游发挥作用。此外,在 Fe 缺乏条件下,bHLH105 和 bHLH115 的转录直接被激活。我们的研究结果为理解 Fe 稳态的调控提供了一个概念框架:IMA 肽通过与 BTS 结合来保护 bHLH105/bHLH115 不被降解,从而激活 Fe 缺乏反应。

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