Functional identification of MdSIZ1 as a SUMO E3 ligase in apple.

J Plant Physiol

State Key Laboratory of Crop Biology, Shandong Agricultural University, Tai-An, Shandong, China; MOA Key Laboratory of Horticultural Crop Biology and Germplasm Innovation, Shandong Agricultural University, Tai-An, Shandong, China; College of Horticulture Science and Engineering, Shandong Agricultural University, Tai-An, Shandong, China. Electronic address:

Published: July 2016

AI Article Synopsis

  • SUMOylation is a process where special proteins called SUMOs attach to other proteins, which helps them work better, and it involves three main types of enzymes: E1, E2, and E3.
  • Researchers found a similar protein called MdSIZ1 in apple plants that works like AtSIZ1 in Arabidopsis, helping with this SUMO process.
  • MdSIZ1 helps apple plants deal with stress from things like temperature changes and other environmental factors by increasing SUMO attachment to key proteins.

Article Abstract

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 (E1), 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 siz1-2 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.

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http://dx.doi.org/10.1016/j.jplph.2016.04.007DOI Listing

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