Citrullination of Proteins as a Specific Response Mechanism in Plants.

Claudius Marondedze, Giuliano Elia, Ludivine Thomas, Aloysius Wong, Christoph A Gehring

Research output: Contribution to journalArticlepeer-review

4 Scopus citations

Abstract

Arginine 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.
Original languageEnglish (US)
JournalFrontiers in plant science
Volume12
DOIs
StatePublished - Apr 26 2021

Bibliographical note

KAUST Repository Item: Exported on 2021-04-29
Acknowledgements: The authors wish to thank Lee Staff for proofreading the manuscript.

ASJC Scopus subject areas

  • Plant Science

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