Open AccessPost‐translational modifications of Arabidopsis E3 SUMO ligase At SIZ 1 are controlled by environmental conditions
Author(s) -
Kim Joo Yong,
Song Jong Tae,
Seo Hak Soo
Publication year - 2017
Publication title -
febs open bio
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.718
H-Index - 31
ISSN - 2211-5463
DOI - 10.1002/2211-5463.12309
Subject(s) - sumo protein , ubiquitin ligase , ubiquitin , arabidopsis , abiotic stress , mutant , abiotic component , dna ligase , microbiology and biotechnology , heat stress , sumo enzymes , chemistry , biology , biochemistry , ecology , enzyme , gene , zoology
Sumoylation regulates numerous cellular functions in plants as well as in other eukaryotic systems. However, the regulatory mechanisms controlling E3 small ubiquitin‐related modifier ( SUMO ) ligase are not well understood. Here, post‐translational modification of the Arabidopsis E3 SUMO ligase At SIZ 1 was shown to be specifically controlled by abiotic stresses. At SIZ 1 ubiquitination was induced by exposure to heat stress in transgenic plants overexpressing the E3 ubiquitin ligase COP 1. In addition, At SIZ 1 ubiquitination was strongly enhanced in transgenic plants overexpressing SUMO isopeptidase ESD 4 under heat stress. By contrast, drought stress induced sumoylation rather than ubiquitination of At SIZ 1 and sumoylated forms of At SIZ 1 accumulated in esd4 and cop1–4 mutants. Moreover, siz1 mutants were found to be tolerant to heat and drought stresses. Taken together, these results indicate that ubiquitination and sumoylation of At SIZ 1 in response to abiotic stresses depend on the activities of COP 1 and ESD 4 and that the activity and stability of At SIZ 1 can be specifically controlled by different abiotic stresses.