Web of Science: 42 cites, Scopus: 43 cites, Google Scholar: cites
Clp protease and OR directly control the proteostasis of phytoene synthase, the crucial enzyme for carotenoid biosynthesis in Arabidopsis
Welsch, Ralf (University of Freiburg. Faculty of Biology II)
Zhou, Xiangjun (Cornell University. Center for Agriculture and Health)
Yuan, Hui (Cornell University. Center for Agriculture and Health)
Álvarez, Daniel (University of Freiburg. Faculty of Biology II)
Sun, Tianhu (Cornell University. Center for Agriculture and Health)
Schlossarek, Dennis (University of Freiburg. Faculty of Biology II)
Yang, Yong (Cornell University. Center for Agriculture and Health)
Shen, Guoxin (Zhejiang Academy of Agricultural Sciences)
Zhang, Hong (Texas Tech University. Department of Biological Sciences)
Rodríguez Concepción, Manuel (Centre de Recerca en Agrigenòmica)
Thannhauser, Theodore W. (Cornell University. Center for Agriculture and Health)
Li, Li (Cornell University. Center for Agriculture and Health)

Data: 2018
Resum: 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.
Nota: Ajuts: This work was supported by Agriculture and Food Research Initiative competitive award no. 2016-67013-24612 from the USDA National Institute of Food and Agriculture and by the HarvestPlus research consortium (2014H6320.FRE)
Drets: Tots els drets reservats
Llengua: Anglès
Document: article ; recerca ; acceptedVersion
Matèria: Carotenoid ; Phytoene synthase ; Clp protease ; OR ; Post-translational regulation ; Arabidopsis
Publicat a: Molecular plant, Vol. 11, Issue 1 (January 2018) , p. 149-162, ISSN 1674-2052

DOI: 10.1016/j.molp.2017.11.003

50 p, 4.9 MB

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 Registre creat el 2018-02-07, darrera modificació el 2020-11-07

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