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dc.contributor.authorMarondedze, Claudius
dc.contributor.authorElia, Giuliano
dc.contributor.authorThomas, Ludivine
dc.contributor.authorWong, Aloysius
dc.contributor.authorGehring, Christoph A
dc.date.accessioned2020-09-14T13:45:55Z
dc.date.available2020-09-14T13:45:55Z
dc.date.issued2020-09-13
dc.identifier.citationMarondedze, 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
dc.identifier.doi10.1101/2020.09.12.294728
dc.identifier.urihttp://hdl.handle.net/10754/665143
dc.description.abstractArginine 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.
dc.description.sponsorshipG.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).
dc.publisherCold Spring Harbor Laboratory
dc.relation.urlhttp://biorxiv.org/lookup/doi/10.1101/2020.09.12.294728
dc.rightsArchived with thanks to Cold Spring Harbor Laboratory
dc.titleArginine citrullination of proteins as a specific response mechanism in Arabidopsis thaliana
dc.typePreprint
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Division
dc.contributor.departmentComputational Bioscience Research Center (CBRC)
dc.contributor.departmentBioscience Core Lab
dc.contributor.departmentComputer, Electrical and Mathematical Sciences and Engineering (CEMSE) Division
dc.contributor.departmentBioscience Program
dc.eprint.versionPre-print
dc.contributor.institutionRijk Zwaan, De Lier 2678 ZG, Netherlands.
dc.contributor.institutionPhilochem AG, Libernstrasse, CH-8112 Otelfingen, Switzerland.
dc.contributor.institutionDepartment of Biology, College of Science and Technology, Wenzhou-Kean University, 88 Daxue Road, Ouhai, Wenzhou, Zhejiang Province 325060, China.
dc.contributor.institutionDepartment of Chemistry, Biology & Biotechnology, University of Perugia, I-06121 Perugia, Italy.
kaust.personMarondedze, Claudius
kaust.personThomas, Ludivine
kaust.personGehring, Christoph A.
refterms.dateFOA2020-09-14T13:47:01Z


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