In the present A work on selective breeding aimed at further consolidation of key qualities of the race of Zalaajinst- Edren white goats towards increased length and fineness of fibers and upgrading phenotypic characteristics (Dorjbat Yo, 2013) resulted i

The present study is focused on the identification of plant proteins, which interact with the newly isolated type A peroxiredoxin protein LeTPx1, using the two-hybrid assay. The leTPx1 cDNA was initially identified as an interacting protein to the glutathione S-transferase/peroxidase BI-GST/GPx (Kampranis, Damianova et al., 2000). The two-hybrid screen is a powerful tool for the characterization of protein-protein interaction using yeast as a model system.To this end, we generated a LexA-LeTPx1 “bait” fusion and screened a tomato library cloned into the activation domain vector pJG4-5. A total of ninety-six interacting cDNAs were isolated, from which 26 were selected for sequencing and further characterization. The majority of the iterators have been previously implicated in stress responses. Due to the interaction observed between LeTPx1 and LeGSTO1 a highly homologous protein to the mammalian GST-Omega, in the yeast two-hybrid system and the potential physiological importance of such an interaction, we proceeded to analyze the biochemical properties of these proteins in vitro. LeGSTO1 was found to posse dehydro-ascorbatereductase activity like its human counterpart. Interestingly, LeGSTO1 was found to be able to reduce an inter-subunit disulfide present in the oxidized form of LeTPx1.The plant GSTO1 homologue was also tested for its ability to inhibit the Bax lethal phenotype in yeast. The plant homologue in contrast with its mammalian counterpart did not suppress the Bax phenotype. In parallel experiments we proceeded to characterize the antioxidant activity of the LeTPx1, the interacting glutathione S-transferases BI-GST/GPx, LeGST-T1, T2, T3, T4, T5 and the mammalian inhibitor of apoptosis Bcl-2.