OsPUB15, an E3 ubiquitin ligase, functions to reduce cellular oxidative stress during seedling establishment

Jong Jin Park, Jakyung Yi, Jinmi Yoon, Lae Hyeon Cho, Jin Ping, Hee Joong Jeong, Seok Keun Cho, Woo Taek Kim, Gynheung An

Research output: Contribution to journalArticlepeer-review

94 Citations (Scopus)


Summary The plant U-box (PUB) protein functions as an E3 ligase to poly-ubiquitinate a target protein for its degradation or post-translational modification. Here, we report functional roles for OsPUB15, which encodes a cytosolic U-box protein in the class-II PUB family. Self-ubiquitination assays showed that bacterially expressed MBP-OsPUB15 protein has E3 ubiquitin ligase activity. A T-DNA insertional mutation in OsPUB15 caused severe growth retardation and a seedling-lethal phenotype. Mutant seeds did not produce primary roots, and their shoot development was significantly delayed. Transgenic plants expressing the OsPUB15 antisense transcript phenocopied these mutant characters. The abnormal phenotypes were partially rescued by two antioxidants, catechin and ascorbic acid. Germinating seeds in the dark also recovered the rootless defect. Levels of H 2O 2 and oxidized proteins were higher in the knock-out mutant compared with the wild type. OsPUB15 transcript levels were increased upon H 2O 2, salt and drought stresses; plants overexpressing the gene grew better than the wild type under high salinity. These results indicate that PUB15 is a regulator that reduces reactive oxygen species (ROS) stress and cell death.

Original languageEnglish
Pages (from-to)194-205
Number of pages12
JournalPlant Journal
Issue number2
Publication statusPublished - 2011 Jan

All Science Journal Classification (ASJC) codes

  • Genetics
  • Plant Science
  • Cell Biology


Dive into the research topics of 'OsPUB15, an E3 ubiquitin ligase, functions to reduce cellular oxidative stress during seedling establishment'. Together they form a unique fingerprint.

Cite this