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    Arginine citrullination of proteins as a specific response mechanism in Arabidopsis thaliana

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    Type
    Preprint
    Authors
    Marondedze, Claudius cc
    Elia, Giuliano
    Thomas, Ludivine
    Wong, Aloysius
    Gehring, Christoph A cc
    KAUST Department
    Biological and Environmental Sciences and Engineering (BESE) Division
    Bioscience Core Lab
    Bioscience Program
    Computational Bioscience Research Center (CBRC)
    Computer, Electrical and Mathematical Sciences and Engineering (CEMSE) Division
    Molecular Signalling Group
    Date
    2020-09-13
    Permanent link to this record
    http://hdl.handle.net/10754/665143
    
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    Abstract
    Arginine citrullination, also referred to as arginine deimination, is a post-translational modification involved in an increasing number of physiological processes in animals, including histone modifications and transcriptional regulation, and in severe diseases such as rheumatoid arthritis and neurodegenerative conditions. It occurs when arginine side chains are deiminated and converted into side chains of the amino acid citrulline, a process catalysed by a family of Ca2+-dependent peptidyl arginine deiminases (PADs). PADs have been discovered in several mammalian species and in other vertebrates, like birds and fish, but have not been observed in bacteria, lower eukaryotes or higher plants. Here we show, firstly, that the Arabidopsis thaliana proteome does contain citrullinated proteins; secondly and importantly, that the citrullination signature changes in response to cold stress. Among the citrullinated proteins are DNA- or RNA-binding proteins thus implying a role for it the control of the transcriptional programming in plant cells. Thirdly, through sequence and structural analysis, we identify one arabidopsis protein, currently annotated as agmatine deiminase (At5g08170), as a candidate protein arginine deiminase. Finally, we show biochemical evidence that AT5G08170 can citrullinate peptides from LHP1-interacting factor 2 (AT4G00830) an RNA-binding protein that has been identified as citrullinated in cell suspension cultures of Arabidopsis thaliana roots. In addition, we show that, in vitro, agmatine deiminase can undergo auto-citrullination. In conclusion, our work established the presence of protein arginine citrullination in higher plants and assigns it a role in post-translational modifications during abiotic stress responses.
    Citation
    Marondedze, C., Elia, G., Thomas, L., Wong, A., & Gehring, C. (2020). Arginine citrullination of proteins as a specific response mechanism in Arabidopsis thaliana. doi:10.1101/2020.09.12.294728
    Sponsors
    G.E. was the recipient of an Erasmus Mundus Action 2, Strand 2, lot 4 (Gulf Countries) award. A.W. was supported by the National Natural Science Foundation of China (31850410470) and the Zhejiang Provincial Natural Science Foundation of China (LQ19C130001).
    Publisher
    Cold Spring Harbor Laboratory
    DOI
    10.1101/2020.09.12.294728
    Additional Links
    http://biorxiv.org/lookup/doi/10.1101/2020.09.12.294728
    ae974a485f413a2113503eed53cd6c53
    10.1101/2020.09.12.294728
    Scopus Count
    Collections
    Biological and Environmental Science and Engineering (BESE) Division; Preprints; Bioscience Program; Computational Bioscience Research Center (CBRC); Bioscience Core Lab; Computer, Electrical and Mathematical Science and Engineering (CEMSE) Division

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