Distinct roles for Arabidopsis SUMO protease ESD4 and its closest homolog ELS1 |
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| Authors: | Rebecca Hermkes Yong-Fu Fu Kerstin Nürrenberg Ruchika Budhiraja Elmon Schmelzer Nabil Elrouby R Jürgen Dohmen Andreas Bachmair George Coupland |
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| Institution: | (1) Department of Plant Developmental Biology, Max Planck Institute for Plant Breeding Research, 50829 Cologne, Germany;(2) Institute for Genetics, University of Cologne, 50674 Cologne, Germany;(3) Central Microscopy, Max Planck Institute for Plant Breeding Research, 50829 Cologne, Germany;(4) Department of Biochemistry and Cell Biology, Max F. Perutz Laboratories, University of Vienna, 1030 Vienna, Austria;(5) Present address: Department of Plant Physiology, Umea Plant Science Centre, Umea University, 90187 Umea, Sweden;(6) Present address: Institute of Crop Sciences, National Key Facility for Crop Gene Resources and Genetic Improvement, Chinese Academy of Agricultural Sciences, Beijing, 100081, People’s Republic of China; |
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| Abstract: | SUMO conjugation affects a broad range of processes in Arabidopsis thaliana, including flower initiation, pathogen defense, and responses to cold, drought and salt stress. We investigated two sequence-related
SUMO-specific proteases that are both widely expressed and show that they differ significantly in their properties. The closest
homolog of SUMO protease ESD4, ESD4-LIKE SUMO PROTEASE 1 (ELS1, alternatively called AtULP1a) has SUMO-specific proteolytic
activity, but is functionally distinct from ESD4, as shown by intracellular localization, mutant phenotype and heterologous
expression in yeast mutants. Furthermore, we show that the growth defects caused by loss of ESD4 function are not due to increased
synthesis of the stress signal salicylic acid, as was previously shown for a SUMO ligase, indicating that impairment of the
SUMO system affects plant growth in different ways. Our results demonstrate that two A. thaliana SUMO proteases showing close sequence similarity have distinct in vivo functions. |
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