UNUSUAL FLORAL ORGAN (UFO), a novel gene, is involved in controlling flowering initiation and development. In Arabidopsis, UFO is required for floral organ identity in the second and third whorls. However, the mode of expression and function of TaUFO have not been studied yet. The cDNA sequence of TaUFO is comprised of 1344 bp open reading frame which encodes 50.82 KDa polypeptide consisting amino acid residues. F-box protein, the components of TaUFO, plays an important regulatory role in a wide diversity of developmental and physiological responses. In almost all F box proteins, the N terminus of the protein contains the F-box motif, and the rest of the protein contains the protein-protein interaction domains required for target protein binding. In order to elucidate the function of the TaUFO, various phytohormones and abiotic stresses were applied on young seedlings (14 day after germination) and its transcripts were evaluated. TaUFO:GFP fusion construct was transformed into onion epidermal cells by particle bombardment to elucidate the subcellular localization of the TaUFO protein. The function of the F-box protein is to interact with target proteins. With the use of a yeast two-hybrid screen to isolate proteins interacting with the TaUFO (F box protein), we identified potential TaUFO interactive protein in wheat spikelet library.

Pectin, one of the main components of plant cell wall, is deesterified in muro by PME (Pectin methylesterase). PME activity is particularly regulated by inhibitor proteins known as the pectin methylesterase inhibitor (PMEI). The PMEI plays a key role in wounding, osmotic stress, senescence and seed development. However, the role of PMEI in plant species still remains to be demonstrated especially in wheat. To facilitate the studies on the expression of the TaPMEI gene, RT-PCR was performed using leaf, stem and root tissues in response to exogeneous application of phytohormones and abiotic stress treatments. Transcription of the TaPMEI gene was significantly induced in NaCl, H2O2 and SA treatments, and reduced when plants were treated with ABA. To elucidate the subcellular localization of the TaPMEI protein, TaPMEI:GFP fusion construct was transformed into onion epidermal cells by particle bombardment. The fluorescence signal was exclusively detected in cell wall of the cells. In order to obtain recombinant TaPMEI protein, the TaPMEI protein, expressed in E.coli as a MBP (~42.5 kDa) fusion protein recombinant. Purification and functinal analysis of TaPMEI as an inhibitor of PME activity are described.