RT Journal Article
SR Electronic
T1 Citrullination of proteins as a specific response mechanism in plants
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 2020.09.12.294728
DO 10.1101/2020.09.12.294728
A1 Claudius Marondedze
A1 Giuliano Elia
A1 Ludivine Thomas
A1 Aloysius Wong
A1 Chris Gehring
YR 2020
UL http://biorxiv.org/content/early/2020/11/21/2020.09.12.294728.abstract
AB Arginine deamination, also referred to as citrullination of proteins by peptidyl-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 Arabidopsis thaliana protein with calcium-dependent arginine deiminase activity. Taken together, these findings establish this post-translational modification as a hitherto neglected component of cellular reprogramming during stress responses.Competing Interest StatementThe authors have declared no competing interest.