Clp Protease and OR Directly Control the Proteostasis of Phytoene Synthase, the Crucial Enzyme for Carotenoid Biosynthesis in Arabidopsis
文献类型: 外文期刊
作者: Welsch, Ralf 1 ; Zhou, Xiangjun 2 ; Yuan, Hui 2 ; Alvarez, Daniel 1 ; Sun, Tianhu 2 ; Schlossarek, Dennis 1 ; Yang, Yo 1 ;
作者机构: 1.Univ Freiburg, Fac Biol 2, D-79104 Freiburg, Germany
2.Cornell Univ, USDA ARS, Robert Holley Ctr Agr & Hlth, Ithaca, NY 14853 USA
3.Cornell Univ, Sch Integrat Plant Sci, Plant Breeding & Genet Sect, Ithaca, NY 14853 USA
4.Zhejiang Acad Agr Sci, Hangzhou 310021, Zhejiang, Peoples R China
5.Texas Tech Univ, Dept Biol Sci, Lubbock, TX 79409 USA
6.Ctr Res Agr Genom CRAG CSIC IRTA UAB UB, Campus UAB Bellaterra, Barcelona, Spain
关键词: carotenoid; phytoene synthase; clp protease; OR; post-translational regulation; Arabidopsis
期刊名称:MOLECULAR PLANT ( 影响因子:13.164; 五年影响因子:16.357 )
ISSN: 1674-2052
年卷期: 2018 年 11 卷 1 期
页码:
收录情况: SCI
摘要: Phytoene synthase (PSY) is the crucial plastidial enzymein the carotenoid biosynthetic pathway. However, its post-translational regulation remains elusive. Likewise, Clp protease constitutes a central part of the plastid protease network, but its substrates for degradation are not well known. In this study, we report that PSY is a substrate of the Clp protease. PSY was uncovered to physically interact with various Clp protease subunits (i.e., ClpS1, ClpC1, and ClpD). High levels of PSY and several other carotenogenic enzyme proteins overaccumulate in the clpc1, clpp4, and clpr1-2 mutants. The overaccumulated PSY was found to be partially enzymatically active. Impairment of Clp activity in clpc1 results in a reduced rate of PSY protein turnover, further supporting the role of Clp protease in degrading PSY protein. On the other hand, the ORANGE (OR) protein, a major post-translational regulator of PSY with holdase chaperone activity, enhances PSY protein stability and increases the enzymatically active proportion of PSY in clpc1, counterbalancing Clp-mediated proteolysis in maintaining PSY proteinhomeostasis. Collectively, these findings provide novel insights into the quality control of plastid-localized proteins and establish a hitherto unidentified post-translational regulatory mechanism of carotenogenic enzymes in modulating carotenoid biosynthesis in plants.
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