1. Proteomic profiling of Arabidopsis nuclei reveals distinct protein accumulation kinetics upon heat stress.
- Author
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Muñoz-Díaz, E., Fuenzalida-Valdivia, I., Darrière, T., de Bures, A., Blanco-Herrera, F., Rompais, M., Carapito, C., and Sáez-Vásquez, J.
- Subjects
LIQUID chromatography-mass spectrometry ,NUCLEAR proteins ,PROTEOMICS ,RNA polymerases ,RIBOSOMAL proteins ,ARABIDOPSIS ,CONTINUOUS groups ,RIBOSOMES - Abstract
Heat stress (HS) impacts the nuclear proteome and, subsequently, protein activities in different nuclear compartments. In Arabidopsis thaliana, a short exposure to 37 °C leads to loss of the standard tripartite architecture of the nucleolus, the most prominent nuclear substructure, and, consequently, affects the assembly of ribosomes. Here, we report a quantitative label-free LC‒MS/MS (Liquid Chromatography coupled to tandem Mass Spectrometry) analysis to determine the nuclear proteome of Arabidopsis at 22 °C, HS (37 °C for 4 and 24 h), and a recovery phase. This analysis identified ten distinct groups of proteins based on relative abundance changes in the nucleus before, during and after HS: Early, Late, Transient, Early Persistent, Late Persistent, Recovery, Early-Like, Late-Like, Transient-Like and Continuous Groups (EG, LG, TG, EPG, LPG, RG, ELG, LLG, TLG and CG, respectively). Interestingly, the RNA polymerase I subunit NRPA3 and other main nucleolar proteins, including NUCLEOLIN 1 and FIBRILLARIN 1 and 2, were detected in RG and CG, suggesting that plants require increased nucleolar activity and likely ribosome assembly to restore protein synthesis after HS. [ABSTRACT FROM AUTHOR]
- Published
- 2024
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