Hou Y M, Kim R, Kim S H
Division of Chemical Biodynamics, Lawrence Berkeley Laboratory, Ca 94720.
Biochim Biophys Acta. 1988 Nov 10;951(1):230-4. doi: 10.1016/0167-4781(88)90045-0.
The cDNA of mouse metallothionein, a small metal-binding protein rich in cysteine, has been cloned downstream from a bacterial inducible promoter and expressed in Escherichia coli. Upon induction, E. coli harboring this cDNA clone contained a protein species readily labelled by [35S]cysteine in vivo and incorporated 10-times as much 109Cd from the medium than would otherwise be the case. We show that expression of metallothionein endows resistance in E. coli to heavy metal ions such as mercury, silver, copper, cadmium and zinc by sequestering rather than exclusion or conversion, common mechanisms of metal resistance in bacteria.
小鼠金属硫蛋白是一种富含半胱氨酸的小型金属结合蛋白,其互补脱氧核糖核酸(cDNA)已被克隆到细菌诱导型启动子下游,并在大肠杆菌中表达。诱导后,携带此cDNA克隆的大肠杆菌含有一种在体内易于被[35S]半胱氨酸标记的蛋白质,并且从培养基中摄取的109镉比正常情况多10倍。我们表明,金属硫蛋白的表达通过螯合而非细菌中常见的金属抗性机制(如排除或转化)赋予大肠杆菌对汞、银、铜、镉和锌等重金属离子的抗性。