Impaired PSII proteostasis triggers a UPR-like response in the var2 mutant of Arabidopsis

© The Author(s) 2019. Published by Oxford University Press on behalf of the Society for Experimental Biology.

Bibliographische Detailangaben
Veröffentlicht in:Journal of experimental botany. - 1985. - 70(2019), 12 vom: 28. Juni, Seite 3075-3088
1. Verfasser: Dogra, Vivek (VerfasserIn)
Weitere Verfasser: Duan, Jianli, Lee, Keun Pyo, Kim, Chanhong
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2019
Zugriff auf das übergeordnete Werk:Journal of experimental botany
Schlagworte:Journal Article Research Support, Non-U.S. Gov't PSII repair Photosystem II damaged protein response proteostasis retrograde signaling singlet oxygen unfolded protein response Photosystem II Protein Complex
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520 |a Cellular protein homeostasis (proteostasis) is maintained through the balance between de novo synthesis and proteolysis. The unfolded/misfolded protein response (UPR) that is triggered by stressed endoplasmic reticulum (ER) also plays an important role in proteostasis in both plants and animals. Although ER-triggered UPR has been extensively studied in plants, the molecular mechanisms underlying mitochondrial and chloroplastic UPRs are largely uncharacterized despite the fact that these organelles are sites of production of harmful reactive oxygen species (ROS), which damage proteins. In this study, we demonstrate that chloroplasts of the Arabidopsis yellow leaf variegation 2 (var2) mutant, which lacks the metalloprotease FtsH2, accumulate damaged chloroplast proteins and trigger a UPR-like response, namely the accumulation of a suite of chloroplast proteins involved in protein quality control (PQC). These PQC proteins include heat-shock proteins, chaperones, proteases, and ROS detoxifiers. Given that FtsH2 functions primarily in photosystem II proteostasis, the accumulation of PQC-related proteins may balance the FtsH2 deficiency. Moreover, the apparent up-regulation of the cognate transcripts indicates that the accumulation of PQC-related proteins in var2 is probably mediated by retrograde signaling, indicating the occurrence of a UPR-like response in var2 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 4 |a PSII repair 
650 4 |a Photosystem II 
650 4 |a damaged protein response 
650 4 |a proteostasis 
650 4 |a retrograde signaling 
650 4 |a singlet oxygen 
650 4 |a unfolded protein response 
650 7 |a Photosystem II Protein Complex  |2 NLM 
700 1 |a Duan, Jianli  |e verfasserin  |4 aut 
700 1 |a Lee, Keun Pyo  |e verfasserin  |4 aut 
700 1 |a Kim, Chanhong  |e verfasserin  |4 aut 
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