Characterization and function of metal ion clusters in metallothionein and metallothionein-like proteins

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Publication Type dissertation
School or College School of Medicine
Department Biochemistry
Author Jensen, Laran T.
Title Characterization and function of metal ion clusters in metallothionein and metallothionein-like proteins
Date 1998-08
Description Metal ions can interact with specific biological molecules and activate or regulate the function of these molecules by causing a change in molecular structure. Metallothioneins (MTs) are small, cysteine rich proteins that bind metal ions tenaciously. Metal ions are chelated within polymetallic clusters and undergo facile metal exchange reactions. MTs appear to function in metal ion regulation and detoxification. Metallothionein-3 (MT-3) is a brain specific member of the metallothionein family of metal binding proteins, and its absence has been implicated in the development of Alzheimer's disease (AD). The growth inhibitory activity of MT-3 appears to result from a distinct amino acid sequence and not unusual metal-binding properties compared with MT-1 or MT-2. The transcription factor Macl from S. cerevisiae regulates the expression of the high affinity copper uptake system in a copper dependent manner. When cells are exposed to copper concentration above starvation levels expression of genes in this uptake system is inhibited. Macl contains two cysteine rich motifs in the C-terminus which resemble Cu(I) binding cysteinyl sequences found in MTs. Macl was found to directly bind Cu(I) ions and a copper dependent intramolecular interaction between the N-terminal DNA binding domain and the C-terminal copper binding activation domain was identified. This interaction may result in the masking of the DNA binding domain in a copper dependent manner abolishing expression of Macl regulated genes. In yeast, MT genes are transcriptionally induced by copper, but not by other metal ions. The primary copper buffering protein in S. cerevisiae is a MT
Type Text
Publisher University of Utah
Subject Yeast; Copper-Binding
Subject MESH Metallothionein; Organometallic Compounds
Dissertation Institution University of Utah
Dissertation Name PhD
Language eng
Relation is Version of Digital reproduction of "Characterization and function of metal ion clusters in metallothionein and metallothionein-like proteins". Spencer S. Eccles Health Sciences Library. Print version of "Characterization and function of metal ion clusters in metallothionein and metallothionein-like proteins". available at J. Willard Marriott Library Special Collection QP6.5 1998 .J46.
Rights Management © Laran T. Jensen.
Format Medium application/pdf
Format Extent 3,146,816 bytes
Identifier undthes,4577
Source Original: University of Utah Spencer S. Eccles Health Sciences Library (no longer available).
Master File Extent 3,146,858 bytes
ARK ark:/87278/s6w37z6j
Setname ir_etd
Date Created 2012-04-24
Date Modified 2021-05-06
ID 191854
Reference URL https://collections.lib.utah.edu/ark:/87278/s6w37z6j