4.7 Article

Functional identification of MdSIZ1 as a SUMO E3 ligase in apple

Journal

JOURNAL OF PLANT PHYSIOLOGY
Volume 198, Issue -, Pages 69-80

Publisher

ELSEVIER GMBH
DOI: 10.1016/j.jplph.2016.04.007

Keywords

Apple; MdSIZ1; SUMO E3 ligase; SUMOylation; Stress responses; Functional complementation

Categories

Funding

  1. National Natural Science Foundation of China [31301763, 31272142]
  2. Foundation for Outstanding Young Scientist in Shandong Province [B52013NY001]
  3. specialized Research Fund for the Doctoral Program of Higher Education of China [20123702120010]

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SUMOylation, the conjugation of target proteins with SUMO (small ubiquitin-related modifier), is a type of post-translational modification in eukaryotes and involves the sequential action of activation (El), conjugation (E2) and ligation (E3) enzymes. In Arabidopsis, the AtSIZ1 protein is a SUMO E3 ligase that promotes the conjugation of SUMO proteins to target substrates. Here, we isolated and identified a SUMO E3 ligase, MdSIZ1, in apple, which was similar to AtSIZ1. SUMOylation analysis showed that MdSIZ1 had SUMO E3 ligase activity in vitro and in vivo. SUMO conjugation was increased by high temperatures, low temperatures, and abscisic acid (ABA). The ectopic expression of MdSIZ1 in Arabidopsis sizl-2 mutant plants partially complemented the morphological mutant phenotype and enhanced the levels of SUMO conjugation. Taken together, these results suggest that MdSIZ1-mediated SUMO conjugation of target proteins is an important process that regulates the adaptation of apple plants to various environmental stresses. (C) 2016 Elsevier GmbH. All rights reserved.

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