ArticleScientific reports2014
Induction of caspase-3-like activity in rice following release of cytochrome-f from the chloroplast and subsequent interaction with the ubiquitin-proteasome system.
Article in Scientific reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 30 citations in OpenAlex.
- Unveiling the "hidden quality" of the walnut pellicle: a precious source of bioactive lipids.Frontiers in plant science · 2024Article
- Initiation and Execution of Programmed Cell Death and Regulation of Reactive Oxygen Species in Plants.International journal of molecular sciences · 2021Review
- Cross-Species Comparisons of Nanoparticle Interactions with Innate Immune Systems: A Methodological Review.Nanomaterials (Basel, Switzerland) · 2021Review
- Cellular oxidative stress in programmed cell death: focusing on chloroplasticJournal of plant research · 2021Article
- Ring/U-Box Protein AtUSR1 Functions in Promoting Leaf Senescence Through JA Signaling Pathway in Arabidopsis.Frontiers in plant science · 2020Article
- Spermidine sprays alleviate the water deficit-induced oxidative stress in finger millet (3 Biotech · 2018Article
- Flavonoids and darkness lower PCD in senescing Vitis vinifera suspension cell cultures.BMC plant biology · 2016Article
- Glucosidase II β-subunit, a novel substrate for caspase-3-like activity in rice, plays as a molecular switch between autophagy and programmed cell death.Scientific reports · 2016Article
- Programmed cell death in plants: A chloroplastic connection.Plant signaling & behavior · 2015Review
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
It has been known that the process of leaf senescence is accompanied by programmed cell death (PCD), and the previous study indicated that dark-induced senescence in detached leaves from rice led to the release of cytochrome f (Cyt f) from chloroplast into the cytoplasm. In this study, the effects of Cyt f on PCD were studied both in vitro and in vivo. In a cell-free system, purified Cyt f activated caspase-3-like protease and endonuclease OsNuc37, and induced DNA fragmentation. Furthermore, Cyt f-induced caspase-3-like activity could be inhibited by MG132, which suggests that the activity was attributed to the 26S proteasome. Conditional expression of Cyt f in the cytoplasm could also activate caspase-3-like activity and DNA fragmentation. Fluorescein diacetate staining and annexin V-FITC/PI double staining demonstrated that Cyt f expression in cytoplasm significantly increased the percentage of PCD protoplasts. Yeast two-hybrid screening showed that Cyt f might interact with E3-ubiquitin ligase and RPN9b, the subunits of the ubiquitin proteasome system (UPS), and other PCD-related proteins. Taken together, these results suggest that the released Cyt f from the chloroplast into the cytoplasm might activate or rescue caspase-3-like activity by interacting with the UPS, ultimately leading to the induction of PCD.
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