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Replacement of all alpha-domain lysines with glutamates reduces metallothionein detoxification function.

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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Cody CW,Huang PC

doi

10.1006/bbrc.1994.2022

subject

Has Abstract

pub_date

1994-07-29 00:00:00

pages

954-9

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(84)72022-5

journal_volume

202

pub_type

杂志文章

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