Characterization of E3 Ligase Ring Finger1 Protein In Wheat.

The RING finger protein is a member of the Zinc finger, consists of four pairs of ligands binding two ions. RING finger proteins are the most abundant proteins in plants, which may be essential for diverse aspects of cellular regulations in plant growth and development. Especially, most RING finger proteins, E3 ubiquitin ligase, play important roles in protein-protein interaction and ubiquitin-dependent protein degradation. Previous reports have provided molecular functions of RING finger genes in several plant species, but little is known about it in wheat. The TaRF1 gene encodes a novel RING finger protein. In this study, we characterized wheat (Triticum aestivum) C3HC4 RING finger as a hexapoid wheat ubiquitin ligase. In order to study the role of TaRF1 in wheat, we isolated TaRF1 from wheat spike cDNA. TaRF1 was 756 bp an encoded a putative protein of 252 amino acids with a predicted molecular mass of 28.57 kDa and an isoelectric point (pI) of 5.75. A typical C3HC4-type RING finger domain was found at the C-terminal region of the TaRF1 protein. The expression of TaRF1 was investigated in developmental stages and various stresses by using RT-PCR. Sub-cellular localization of TaRF1 using green fluorescent protein (GFP) reporters was confirmed. TaRF1-interacting proteins via yeast two-hybrid screening are proposed.

Acknowledgement : This research was supported by the Technology Development Program for Agriculture and Forestry, Ministry for Food, Agriculture, Forestry and Fisheries, Republic of Korea.