中文摘要：

以pGEX-KG为骨架，运用分子克隆方法构建了生长素结合蛋白AtTIR1和IAA28的原核表达载体，通过转化不同表达菌株探索了2种蛋白的诱导表达条件。结果表明：在0．4mmol／LIPTG诱导下，GST-IAA28融合蛋白在表达菌株Tuner中的表达量最高，其适宜诱导温度为16℃；在0．6mmo ULIPTG诱导下，BL21（DE3）中GST-IAA28的表达量最高；在各种浓度的IPTG诱导下，Rosetta中的GST-IAA28的产量均不高；在25℃和0．4mmol／LIPTG诱导条件下，Rosetta中的GST-AtTIR1表达总量最高，每克细菌可诱导出约0．2mg的目标蛋白，但BL21（DE3）菌种中的GST-AtTIR1表达量很低。利用GST Sefirose^TM resin亲和树脂对表达的蛋白进行纯化，获得了较纯的AtTIRl和IAA28蛋白。

英文摘要：

Prokaryotic expression vector of auxin-binding protein AtTIR1 and IAA28 were constructed by gene cloning based on pGEX-KG. The expression induction conditions of two kinds of different expression strains after transfected with the recombined expression vectors were investigated. The results showed that the GST-IAA28 had the highest yields in Tuner under 0.4 mmol/L IPTG and the highest yields in BL21（DE3） at 0.6 mmol/L IPTG~ with 16 ~C the suitable inducing temperature, while the protein yields were low in Rosetta under every concentration of IPTG. GST-AtTIR1 expressed highly in Rosetta at the optimal induced condition of 0.4 mmol/L IPTG and 25 ℃, and about 0.2 mg GST-AtTIR1 was produced in lg bacteria. But GST-AtTIR1 expressed lowly in BL21. Meanwhile, relatively purified GST-AtTIR1 and GST-IAA28 had been obtained through GST SefiroseTM resin.