Work

Replacement of All α-Domain Lysines with Glutamates Reduces Metallothionein Detoxification Function

Year: 1994

Type: article

Abstract: Mammalian metallothioneins (MTs) possess eight highly conserved lysine residues, including three in each of two metal binding domains. We used site-directed mutagenesis to replace these intradomain lysines in Chinese hamster ovary MT2 with glutamic acid and/or glutamine. These mutant MTs were expressed in a metal sensitive yeast host. One mutant which had all three lysines in the alpha-domain replaced by glutamates (K43,51,56E) exhibited a reduced ability, relative to native MT, to protect yeast transformants against otherwise toxic levels of cadmium. This triply substituted mutant also exhibited anomalous migration on a non-denaturing gel relative to wild type MT and other MT lysine mutants, suggesting that the intradomain lysines are important in maintaining the conformational integrity of MT.

Source: Biochemical and Biophysical Research Communications

DOI: 10.1006/bbrc.1994.2022

Authors: C.W. Cody, P.C. Huang

Institution: Johns Hopkins University

Language: English

Topic: Trace Elements in Health

Subfield: Nutrition and Dietetics

Field: Nursing

Domain: Health Sciences

Open Access status: hybrid

Estimated APC paid: $3,110

Funders: National Institutes of Health, National Institute of General Medical Sciences