【摘要】 为探究藏桃精氨酸酶1的耐逆性生物学功能，克隆了精氨酸酶1基因（AmArg1）全长ORF,用生物信息学技术分析其蛋白结构和理化性质，结果表明，该蛋白是酸性的无信号肽结构的非分泌蛋白。将AmArg1转入酵母细胞，其对酵母细胞无毒性、无自激活活性。通过酵母双杂交技术筛选出AmArg1的互作蛋白AmLhcb1、AmRabB1b并在洋葱活体细胞内验证互作，并初步探究AmArg1在NaCl、甘露醇和CuSO₄胁迫下的抗逆性反应，发现过表达转AmArg1酵母菌具有较强的胁迫耐受性。更多还原

【Abstract】 In order to investigate the arginase 1（AmArg1） of Amygdalus mira, the full-length ORF of the arginase 1,AmArg1was cloned and therefore, the deduced protein sequence was predicted for structure and physicochemical properties via bioinformatics analysis. The results showed that the protein was an acidic, non-secreted protein with no signal peptide structure. AmArg1 was transferred into yeast cells and it was non-toxic and non-self-activating for yeast cells. The interacting proteins, AmLhcb1 and AmRabB1b of AmArg1 were screened by yeast two hybrid assays, and their interactions were validated by BiFC analysis. Transgenic yeast in response to NaCl, mannitol, and CuSO₄ stress was preliminarily explored, and found that over-expression of AmArg1 might increase the tolerance to these stresses.更多还原