| Summary: | 碩士 === 慈濟大學 === 醫學生物技術研究所 === 95 === hSecurin (encoding the pituitary tumor–transforming 1 protein, PTTG1) is a cell-cycle regulated protein, which main function is to regulate the separation of sister chromatid. hSecurin has been found to associate with other proteins such as separase, a sister-chromatid protein, p53, a tumor suppressor, and Ku, the regulatory subunit of DNA-dependent protein kinase, etc. The function of hSecurin can be divided into two domains, N-terminus and C-terminus. The N-terminus of hSecruin can interact with p53 and inhibit the apotosis, and the C-terminus works as transcriptional factor. In this, we cloned, expressed and purified the full-length, N-terminal 1-120 and C-terminal 108-202 of hSecurin, and investigated their structural properties under various conditions, including pH values. Our results indicated that full-length hSecurin is not a partially unfolded protein. It showed different secondary structure compositions under different pH conditions. C-terminus of hSecurin showed a similar structural manner as full-length hSecurin. N-terminus of hSecurin may involve in reduce hSecurin structure before ubiquitination-dependent proteolysis.
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