作　　者： ; ; ;

机构地区： 北京大学生命科学学院

出　　处： 《生物化学与生物物理进展》 1996年第3期237-239,共3页

摘　　要： 单细胞蓝藻中的类金属硫蛋白已经得到分离纯化，并在蛋白质水平上与标准的哺乳动物金属硫蛋白做了对比性分析，发现二者氨基酸组成和序列差异很大，前者只形成一个结构域，但二级结构和金属结合性质具有一定的相似性，是进化上功能趋同的表现．同时克隆并分析了它的基因ＯＲＦ结构，研究了金属诱导和逆向转录抑制对于蛋白质表达的调控及类似于哺乳动物金属硫蛋白基因具有的放大和重排现象机理，提出了近期研究的重点和方向． Unicellular cyanobacterium metallothionein (MT-like) has been isolated and analyzed comparing with mammal MT. Although there are many differences on their amino acid composition, primary sequence and domain numbers of tertiary structure, their secondary structure and metal-binding properties are similar to each other, showing a kind of function-trending evolution. The MT-like gene: smt-locus has alsobeen cloned and studied about smt A ORF structure, expressional regulation by metal inducing and smt B reverse-transcripted inhibiting, and about the mechanism of the smt genetic amplification and rearrangment as mammal MT genetic unit. Some questions and focal points about cyanobacterium MT-like studying are suggested.

关 键 词： 蓝藻 类金属硫蛋白

领　　域： [生物学]