ArticleScientific reports2019
Accumulation of protein aggregates induces autolytic programmed cell death in hybrid tobacco cells expressing hybrid lethality.
Article in Scientific reports, 2019. 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, 21 citations in OpenAlex.
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- A recessive LRR-RLK gene causes hybrid breakdown in cotton.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2023Article
- The plant trans-Golgi network component ECHIDNA regulates defense, cell death, and endoplasmic reticulum stress.Plant physiology · 2023Article
- The RPN12a proteasome subunit is essential for the multiple hormonal homeostasis controlling the progression of leaf senescence.Communications biology · 2022Article
- Cross-kingdom transcriptomic trends in the evolution of hybrid gene expression.Journal of evolutionary biology · 2022Article
- Phenylalanine ammonia-lyase and phenolic compounds are related to hybrid lethality in the crossPlant biotechnology (Tokyo, Japan) · 2020Article
- Caffeine and NADAntioxidants (Basel, Switzerland) · 2020Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hybrid cells of Nicotiana suaveolens x N. tabacum grow normally at 36 °C, but immediately express lethality due to probable autoimmune response when transferred from 36 to 28 °C. Our recent study showed that the temperature-sensitive lethality of these hybrid cells occurs through autolytic programmed cell death (PCD). However, what happens in hybrid cells following the induction of autoimmune response to autolytic PCD is unclear. We hypothesized that accumulation of protein aggregates in hybrid cells induces autolytic PCD and examined detergent-insoluble protein (protein aggregates) isolated from hybrid cells expressing lethality. The amount of insoluble proteins increased in hybrid cells. Sodium 4-phenylbutyrate, a chemical chaperone, inhibited both the accumulation of insoluble proteins and irreversible progression of cell death. In contrast, E-64, a cysteine protease inhibitor, accelerated both the accumulation of insoluble proteins and cell death. Moreover, proteome analysis revealed that proteasome-component proteins were accumulated specifically in cells treated with E-64, and proteasome activity of hybrid cells decreased after induction of lethality. These findings demonstrate that accumulation of protein aggregates, including proteasome subunits, eventually cause autolytic PCD in hybrid cells. This suggests a novel process inducing plant PCD by loss of protein homeostasis and provides clues to future approaches for elucidating the whole process.
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