Citrullination of proteins as a specific response mechanism in plants
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,...
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Frontiers Media
2022
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| Online Access: | https://www.frontiersin.org/articles/10.3389/fpls.2021.638392/full http://hdl.handle.net/11408/4741 |
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| author | Marondedze, Claudius Elia, Giuliano Thomas, Ludivine Wong, Aloysius Gehring, Chris |
| author_facet | Marondedze, Claudius Elia, Giuliano Thomas, Ludivine Wong, Aloysius Gehring, Chris |
| author_sort | Marondedze, Claudius |
| collection | DSpace |
| description | 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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| id | ir-11408-4741 |
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| language | English |
| publishDate | 2022 |
| publisher | Frontiers Media |
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| spelling | ir-11408-47412022-06-27T13:49:06Z Citrullination of proteins as a specific response mechanism in plants Marondedze, Claudius Elia, Giuliano Thomas, Ludivine Wong, Aloysius Gehring, Chris citrullination proteins response mechanism plants 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. 2022-03-24T13:49:23Z 2022-03-24T13:49:23Z 2021 Article 1664-462X https://www.frontiersin.org/articles/10.3389/fpls.2021.638392/full http://hdl.handle.net/11408/4741 en Frontiers in Plant Science;Vo.12 open Frontiers Media |
| spellingShingle | citrullination proteins response mechanism plants Marondedze, Claudius Elia, Giuliano Thomas, Ludivine Wong, Aloysius Gehring, Chris Citrullination of proteins as a specific response mechanism in plants |
| title | Citrullination of proteins as a specific response mechanism in plants |
| title_full | Citrullination of proteins as a specific response mechanism in plants |
| title_fullStr | Citrullination of proteins as a specific response mechanism in plants |
| title_full_unstemmed | Citrullination of proteins as a specific response mechanism in plants |
| title_short | Citrullination of proteins as a specific response mechanism in plants |
| title_sort | citrullination of proteins as a specific response mechanism in plants |
| topic | citrullination proteins response mechanism plants |
| url | https://www.frontiersin.org/articles/10.3389/fpls.2021.638392/full http://hdl.handle.net/11408/4741 |
| work_keys_str_mv | AT marondedzeclaudius citrullinationofproteinsasaspecificresponsemechanisminplants AT eliagiuliano citrullinationofproteinsasaspecificresponsemechanisminplants AT thomasludivine citrullinationofproteinsasaspecificresponsemechanisminplants AT wongaloysius citrullinationofproteinsasaspecificresponsemechanisminplants AT gehringchris citrullinationofproteinsasaspecificresponsemechanisminplants |