The E3 ligase AtRDUF1 positively regulates salt stress responses in Arabidopsis thaliana

PLoS One. 2013 Aug 12;8(8):e71078. doi: 10.1371/journal.pone.0071078. eCollection 2013.

Abstract

Ubiquitination is an important post-translational protein modification that is known to play critical roles in diverse biological processes in eukaryotes. The RING E3 ligases function in ubiquitination pathways, and are involved in a large diversity of physiological processes in higher plants. The RING domain-containing E3 ligase AtRDUF1 was previously identified as a positive regulator of ABA-mediated dehydration stress response in Arabidopsis. In this study, we report that AtRDUF1 is involved in plant responses to salt stress. AtRDUF1 expression is upregulated by salt treatment. Overexpression of AtRDUF1 in Arabidopsis results in an insensitivity to salt and osmotic stresses during germination and seedling growth. A double knock-out mutant of AtRDUF1 and its close homolog AtRDUF2 (atrduf1atrduf2) was hypersensitive to salt treatment. The expression levels of the stress-response genes RD29B, RD22, and KIN1 are more sensitive to salt treatment in AtRDUF1 overexpression plants. In summary, our data show that AtRDUF1 positively regulates responses to salt stress in Arabidopsis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Arabidopsis / physiology*
  • Arabidopsis Proteins / chemistry
  • Arabidopsis Proteins / genetics*
  • Arabidopsis Proteins / metabolism*
  • Gene Expression
  • Gene Expression Regulation, Plant / drug effects
  • Molecular Sequence Data
  • Organ Specificity / genetics
  • Osmotic Pressure
  • Phenotype
  • Protein Interaction Domains and Motifs
  • Salt Tolerance / genetics*
  • Sequence Alignment
  • Sodium Chloride / pharmacology
  • Stress, Physiological*
  • Ubiquitin-Protein Ligases / chemistry
  • Ubiquitin-Protein Ligases / genetics*
  • Ubiquitin-Protein Ligases / metabolism*

Substances

  • Arabidopsis Proteins
  • Sodium Chloride
  • RDUF1 protein, Arabidopsis
  • Ubiquitin-Protein Ligases

Grants and funding

This work was supported by the Program from the Chinese Ministry of Agriculture (2011ZX0 8009-003-002), the Natural Science Foundation of China for the innovation team (31121065) and the Innovation Grant of CAS (KSCX2-EW-N-07-3). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.