Journal
PLANT CELL AND ENVIRONMENT
Volume 40, Issue 11, Pages 2644-2662Publisher
WILEY
DOI: 10.1111/pce.12994
Keywords
Arabidopsis; thaliana; dry weight; LSD1; oxidative stress; protein interaction; transcription regulation
Categories
Funding
- 'Maestro 6' project [2014/14/A/NZ1/00218]
- National Science Centre
- 'Warsaw Plant Health Initiative' operating within the 7th EU Framework Programme [FP7-REGPOT-2012-1-286093]
- FWO project [G0D7914N]
- WOODTECH project - National Centre for Research and Development [PBS1/A8/16/2013]
- Biostrateg (CROPTECH) project - National Centre for Research and Development [298241]
- Foundation for Polish Science [START 126.2014]
- postdoctoral fellow of 'A program to improve the level of the didactic approach to the question of how to obtain raw plant materials for the purposes of energy production in the context of the Europe Strategy objectives' project [POKL.04.03.00-00-042/12-00]
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Since its discovery over two decades ago as an important cell death regulator in Arabidopsis thaliana, the role of LESION SIMULATING DISEASE 1 (LSD1) has been studied intensively within both biotic and abiotic stress responses as well as with respect to plant fitness regulation. However, its molecular mode of action remains enigmatic. Here, we demonstrate that nucleo-cytoplasmic LSD1 interacts with a broad range of other proteins that are engaged in various molecular pathways such as ubiquitination, methylation, cell cycle control, gametogenesis, embryo development and cell wall formation. The interaction of LSD1 with these partners is dependent on redox status, as oxidative stress significantly changes the quantity and types of LSD1-formed complexes. Furthermore, we show that LSD1 regulates the number and size of leaf mesophyll cells and affects plant vegetative growth. Importantly, we also reveal that in addition to its function as a scaffold protein, LSD1 acts as a transcriptional regulator. Taken together, our results demonstrate that LSD1 plays a dual role within the cell by acting as a condition-dependent scaffold protein and as a transcription regulator.
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