Elevated Temperature Effects on Protein Turnover Dynamics in Arabidopsis thaliana Seedlings Revealed by 15N-Stable Isotope Labeling and ProteinTurnover Algorithm

Author:

Fan Kai-Ting1ORCID,Xu Yuan2,Hegeman Adrian D.3

Affiliation:

1. Agricultural Biotechnology Research Center, Academia Sinica, Taipei 115, Taiwan

2. MSU-DOE Plant Research Laboratory, Michigan State University, East Lansing, MI 48824, USA

3. Departments of Horticultural Science and Plant and Microbial Biology, University of Minnesota, Twin Cities, MN 55108, USA

Abstract

Global warming poses a threat to plant survival, impacting growth and agricultural yield. Protein turnover, a critical regulatory mechanism balancing protein synthesis and degradation, is crucial for the cellular response to environmental changes. We investigated the effects of elevated temperature on proteome dynamics in Arabidopsis thaliana seedlings using 15N-stable isotope labeling and ultra-performance liquid chromatography-high resolution mass spectrometry, coupled with the ProteinTurnover algorithm. Analyzing different cellular fractions from plants grown under 22 °C and 30 °C growth conditions, we found significant changes in the turnover rates of 571 proteins, with a median 1.4-fold increase, indicating accelerated protein dynamics under thermal stress. Notably, soluble root fraction proteins exhibited smaller turnover changes, suggesting tissue-specific adaptations. Significant turnover alterations occurred with redox signaling, stress response, protein folding, secondary metabolism, and photorespiration, indicating complex responses enhancing plant thermal resilience. Conversely, proteins involved in carbohydrate metabolism and mitochondrial ATP synthesis showed minimal changes, highlighting their stability. This analysis highlights the intricate balance between proteome stability and adaptability, advancing our understanding of plant responses to heat stress and supporting the development of improved thermotolerant crops.

Funder

NSF Plant Genome Research Program

Office of Basic Energy Sciences at the U.S. Department of Energy

National Institutes of Health

Minnesota Agricultural Experiment Station

Publisher

MDPI AG

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