Tsiboli P, Triantafillidou D, Franceschi F, Choli-Papadopoulou T
Laboratory of Biochemistry, School of Chemistry, Aristotle University of Thessaloniki, Greece.
Eur J Biochem. 1998 Aug 15;256(1):136-41. doi: 10.1046/j.1432-1327.1998.2560136.x.
The S14 ribosomal protein from the thermophilic organism Thermus thermophilus, which contains a zinc-finger-like motif, namely -C-X2-C-X12-C-X2-C- [Tsiboli, P. & Choli, T. (1995) Biol. Chem. Hoppe-Seyler 376, 127-130], has been overproduced, purified and investigated for its zinc content. According to atomic absorption experiments, the protein contains zinc at a molar ratio of one. Denaturation experiments with simultaneous use of denaturing and chelating agents (guanidine hydrochloride and EDTA), as well as renaturation experiments, have shown both that Zn is strongly bound to the protein and with 1:1 Zn/protein stoicheiometry. These findings provide very strong evidence in support of the participation of the zinc-finger motif and the Zn in the formation of a zinc-finger domain.
嗜热栖热菌的S14核糖体蛋白含有一个类锌指基序，即-C-X2-C-X12-C-X2-C- [齐博利，P. & 乔利，T. (1995) 《生物化学. 霍佩-赛勒》376, 127 - 130]，该蛋白已大量表达、纯化并对其锌含量进行了研究。根据原子吸收实验，该蛋白含锌的摩尔比为1:1。同时使用变性剂和螯合剂（盐酸胍和乙二胺四乙酸）进行的变性实验以及复性实验均表明，锌与该蛋白紧密结合，且锌/蛋白化学计量比为1:1。这些发现为锌指基序和锌参与锌指结构域的形成提供了非常有力的证据。
