ABSTRACT
Importance of dedicated web servers and specialized software for simulations of protein-protein interactions is well established. The purpose of our study was to examine the protein-protein interaction that occurred under physiological and stress conditions between peroxiredoxin II and the creatine kinase brain-type using protein-docking server ClusPro 2.0. To predict the particular site of amino acid docking, computer software analyzes various protein conformations and chooses the most profitable energy state, therefore selecting a number of possible combinations that would fit the correct profile. By co-immunoprecipitation assay, we demonstrated that two molecules Prx II and CKBB have interacted with further attenuation of this specific binding by pretreatment with selected stress factors. In previous study, we showed that the enzymatic activity of CKBB was recovered by different concentration ratios of Prx II. The specific binding models were generated by ClusPro 2.0 protein docking server and studied using PyMol software. It was shown that a number of amino acid residues including Lys 11, Arg 13, Ala 204, Arg 209for creatine kinase, and Asp 181, Glu 192, Lys 196, Glu 162, Gln 163 for Prx II have participated in the complex formation throughout the first ten conformations.
ABSTRACT
Objective In this study, we investigated the distribution of Peroxiredoxin II mRNA in follicles at all stages in mouse ovaries and mouse secondary oocytes(MII eggs) basing on our previous researches, to provide the morphological basis for exploring the effect of Peroxiredoxin II on oogenesis and oocyte maturation in the mouse. Methods To observe the distribution of Peroxiredoxin II mRNA in follicles at all stages in ovaries and the localization of Peroxiredoxin II mRNA in Germinal-Vesicle intact oocytes(GV oocytes) and MII eggs by in situ Hybridization. Results In situ hybridization of ovary section revealed that the signals for Peroxiredoxin II mRNA were undetectable in oocytes of primordial follicles, and moderate signals for Peroxiredoxin II mRNA were observed in oocytes of primary follicles. Moreover, strong signals for Peroxiredoxin II mRNA were evident in antral follicles. The signals for Peroxiredoxin II mRNA also existed in GV oocytes and MII eggs in vitro. The hybrid signals were stronger in GV oocytes than in MII eggs. In addition, the weak but consistent signals for Peroxiredoxin II mRNA were detected in follicular cells from primordial follicles to large antral follicles. Peroxiredoxin II mRNA was located in cytoplasm of oocytes and follicular cells, but not in nuclei.Conclusion These results suggested that Peroxiredoxin II might be involved in the regulation of oogenesis and oocyte matruation in the mouse.;