Proteomic analysis of the regulatory networks of ClpX in a model cyanobacterium Synechocystis sp. PCC 6803.

Proteomic analysis of the regulatory networks of ClpX in a model cyanobacterium Synechocystis sp. PCC 6803.
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蓝藻集胞藻模型中 ClpX 调控网络的蛋白质组学分析。

DOI:
10.3389/fpls.2022.994056
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发表时间:
2022
影响因子:
5.6
通讯作者:
--
中科院分区:
生物学2区
文献类型:
--
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蛋白质稳态受到蛋白质质量控制系统(如伴侣蛋白和蛋白酶)的严格调控。在蓝藻中,ClpXP蛋白水解复合物被认为是一个具有代表性的蛋白水解系统,它由一个六聚体atp酶ClpX和一个四聚体肽酶ClpP组成。然而,ClpX在蓝藻中的功能和分子机制尚不清楚。本研究旨在揭示ClpX在模式蓝藻Synechocystis sp. PCC 6803(以下简称Synechocystis)中的独特作用和调控网络。我们发现clpX的中断导致生长缓慢,高耐光性降低,光合循环电子转移受损。采用定量蛋白质组学策略来全局鉴定聚囊藻细胞中clpx调节的蛋白。在clpX中断后,我们共鉴定出172个差异表达蛋白(DEPs)。功能分析表明,这些DEPs参与多种生物过程,包括糖酵解、氮同化、光合电子传递、atp结合盒(ABC)转运体和双组分信号转导。平行反应监测(PRM)分析证实了24个DEPs的表达。特别是,许多假设的或未知的蛋白被发现受ClpX调控,为未来ClpX的功能研究提供了新的候选蛋白。总之,我们的研究提供了一个全面的clpx调节的蛋白质网络,结果为了解蓝藻中的蛋白质质量控制系统提供了重要的资源。
Protein homeostasis is tightly regulated by protein quality control systems such as chaperones and proteases. In cyanobacteria, the ClpXP proteolytic complex is regarded as a representative proteolytic system and consists of a hexameric ATPase ClpX and a tetradecameric peptidase ClpP. However, the functions and molecular mechanisms of ClpX in cyanobacteria remain unclear. This study aimed to decipher the unique contributions and regulatory networks of ClpX in the model cyanobacterium Synechocystis sp. PCC 6803 (hereafter Synechocystis). We showed that the interruption of clpX led to slower growth, decreased high light tolerance, and impaired photosynthetic cyclic electron transfer. A quantitative proteomic strategy was employed to globally identify ClpX-regulated proteins in Synechocystis cells. In total, we identified 172 differentially expressed proteins (DEPs) upon the interruption of clpX. Functional analysis revealed that these DEPs are involved in diverse biological processes, including glycolysis, nitrogen assimilation, photosynthetic electron transport, ATP-binding cassette (ABC) transporters, and two-component signal transduction. The expression of 24 DEPs was confirmed by parallel reaction monitoring (PRM) analysis. In particular, many hypothetical or unknown proteins were found to be regulated by ClpX, providing new candidates for future functional studies on ClpX. Together, our study provides a comprehensive ClpX-regulated protein network, and the results serve as an important resource for understanding protein quality control systems in cyanobacteria.
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