Shi J, Lindsay W P, Huckle J W, Morby A P, Robinson N J
Department of Biological Sciences, University of Durham, UK.
FEBS Lett. 1992 Jun 1;303(2-3):159-63. doi: 10.1016/0014-5793(92)80509-f.
The recently isolated Synechococcus gene smtA encodes the only characterised prokaryotic protein designated to be a metallothionein (MT). To examine the metal-binding properties of its product the smtA gene was expressed in Escherichia coli as a carboxyterminal extension of glutathione-S-transferase. The pH of half dissociation of Zn, Cd and Cu ions from the expressed protein was determined to be 4.10, 3.50, 2.35, respectively, indicating a high affinity for these ions (in particular for Zn in comparison to mammalian MT). E. coli expressing this gene showed enhanced (ca. 3-fold) accumulation of Zn.
最近分离出的集胞藻属基因smtA编码了唯一一种被鉴定为金属硫蛋白(MT)的原核生物蛋白质。为了检测其产物的金属结合特性,smtA基因在大肠杆菌中作为谷胱甘肽-S-转移酶的羧基末端延伸片段进行表达。所表达蛋白质中锌、镉和铜离子的半数解离pH值分别测定为4.10、3.50和2.35,表明其对这些离子具有高亲和力(特别是与哺乳动物MT相比,对锌的亲和力更高)。表达该基因的大肠杆菌显示锌的积累增强(约3倍)。