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Citrullination of Proteins as a Specific Response Mechanism in Plants.
Marondedze, Claudius; Elia, Giuliano; Thomas, Ludivine; Wong, Aloysius; Gehring, Chris.
Afiliación
  • Marondedze C; Division of Biological and Chemical Science and Engineering, King Abdullah University of Science and Technology, Thuwal, Saudi Arabia.
  • Elia G; Rijk Zwaan, De Lier, Netherlands.
  • Thomas L; Department of Biochemistry, Faculty of Medicine, Midlands State University, Gweru, Zimbabwe.
  • Wong A; Conway Institute of Biomolecular and Biomedical Research, University College Dublin, Dublin, Ireland.
  • Gehring C; Division of Biological and Chemical Science and Engineering, King Abdullah University of Science and Technology, Thuwal, Saudi Arabia.
Front Plant Sci ; 12: 638392, 2021.
Article en En | MEDLINE | ID: mdl-33897727
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.
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Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Tipo de estudio: Prognostic_studies Idioma: En Revista: Front Plant Sci Año: 2021 Tipo del documento: Article País de afiliación: Arabia Saudita

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Tipo de estudio: Prognostic_studies Idioma: En Revista: Front Plant Sci Año: 2021 Tipo del documento: Article País de afiliación: Arabia Saudita