The cysteine-to-histidine substitution in domain of metallothionein enhances its zinc binding ability

Title:The cysteine-to-histidine substitution in domain of metallothionein enhances its zinc binding ability

Volume: 7 Issue: 1

Author(s): Yanjiao Zhou, Ning Zhang, Lingyuan Li and Binggen Ru*

Affiliation:

• National Laboratory of Protein Engineering, Peking University Beijing 100871, P.R.China

Abstract: A two-step PCR method was taken to replace the cysteines at position 19, 29 in p domain of Metallothionein with histidines. Then the His19·29-mutant fragment was cloned into the vector pGEX-4T-l and expressed as a fusion protein of glutathione-S-transferase. After cleaved with thrombin and purified, the p domain with the substitution of Cys-to-His was obtained and identified by amino acid composition and molecular weight. The His19·29 mutant can bind with the same amount of zinc or cadmium ions as the p domain but exhibits stronger zinc binding ability and weaker cadmium binding ability.

Cite this article as:

Zhou Yanjiao, Zhang Ning, Li Lingyuan and Ru Binggen*, The cysteine-to-histidine substitution in domain of metallothionein enhances its zinc binding ability, Protein & Peptide Letters 2000; 7 (1) . https://dx.doi.org/10.2174/092986650701221205145829