Citrullination of Proteins as a Specific Response Mechanism in Plants.
KAUST DepartmentBiological and Environmental Sciences and Engineering (BESE) Division
Computational Bioscience Research Center (CBRC)
Bioscience Core Lab
Computer, Electrical and Mathematical Sciences and Engineering (CEMSE) Division
Permanent link to this recordhttp://hdl.handle.net/10754/668990
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AbstractArginine deimination, also referred to as citrullination of proteins by L-arginine deiminases, is a post-translational modification affecting histone modifications, epigenetic transcriptional regulation, and proteolysis in animals but has not been reported in higher plants. Here we report, firstly, that Arabidopsis thaliana proteome contains proteins with a specific citrullination signature and that many of the citrullinated proteins have nucleotide-binding regulatory functions. Secondly, we show that changes in the citrullinome occur in response to cold stress, and thirdly, we identify an A. thaliana protein with peptidyl arginine deiminase activity that was shown to be calcium-dependent for many peptide substrates. Taken together, these findings establish this post-translational modification as a hitherto neglected component of cellular reprogramming during stress responses.
CitationMarondedze, C., Elia, G., Thomas, L., Wong, A., & Gehring, C. (2021). Citrullination of Proteins as a Specific Response Mechanism in Plants. Frontiers in Plant Science, 12. doi:10.3389/fpls.2021.638392
SponsorsThe authors wish to thank Lee Staff for proofreading the manuscript.
GE was the recipient of an Erasmus Mundus Action 2, Strand 2, and lot 4 (Gulf Countries) award. AW was supported by the National Natural Science Foundation of China (31850410470) and the Zhejiang Provincial Natural Science Foundation of China (LQ19C130001).
PublisherFrontiers Media SA
JournalFrontiers in plant science
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