Functional comparision between truncated MTT1 and truncated MTT2 from Tetrahyemna thermophila. Issue 3 (4th March 2018)

• Record Type: Journal Article
• Authors: Zhou, Huanxin; Xu, Jing; Wang, Wei
• Is Part Of: Bioscience, biotechnology, and biochemistry. Volume 82:Issue 3(2018)
• Page Start: 449
• Page End: 455
• Publication Date: 2018-03-04
• Subjects: Tetrahymena -- metallothionein -- cadmium -- cupper; Biotechnology -- Periodicals; Biochemistry -- Periodicals; 660.6
• DOI: 10.1080/09168451.2018.1431517
• Languages: English
• ISSNs: 0916-8451

Abstract

Abstract: Metallothioneins (MTs) are low-molecular-weight proteins with high Cys content and high metal-chelating ability. CdMT and CuMT subfamilies present different characteristics in Tetrahymena . To explore the effect of the cysteine arrangement and sequence length of MTs for binding different metal ions, MTT1, truncated MTT1 ( TM1 ), MTT2, and truncated MTT2 (TM2) were expressed in E. coli . The half-maximal inhibiting concentrations (IC50 ) of Cd 2+ and Cu + for the recombinant strains were different. Furthermore, E. coli cells expressing MTT1 and TM1 exhibited higher accumulating ability for Cd 2+ than cells expressing MTT2 and TM2. However, the opposite is true for Cu + . The binding ability of the different recombinant proteins to Cd 2+ and Cu + were also different. MTT1 and truncated mutant TM1 were the preference for Cd 2+, whereas MTT2 and truncated mutant TM2 were the preference for Cu + coordination. These results showed that metal ion tolerance and accumulation ability not only depended on cysteine arrangement pattern but also on sequence length of MT in Tetrahymena . Abstract: : Accumulation of metal ion Cd 2+ and Cu + in MT transformed cells.