Purification and characterization of a protein that binds to metal responsive elements of the human metallothionein IIA gene

• Published in: The Journal of biological chemistry Vol. 269; no. 38; pp. 23700 - 23707
• Main Authors: Otsuka, F, Iwamatsu, A, Suzuki, K, Ohsawa, M, Hamer, D H, Koizumi, S
• Format: Journal Article
• Language: English
• Published: United States American Society for Biochemistry and Molecular Biology 23.09.1994
• Subjects: Amino Acid Sequence; Base Sequence; Binding Sites; DNA-Binding Proteins - metabolism; Gene Expression Regulation; HeLa Cells; Humans; Metallothionein - genetics; Molecular Sequence Data; Molecular Weight; Nuclear Proteins - chemistry; Nuclear Proteins - isolation & purification; Nuclear Proteins - metabolism; Oligonucleotide Probes - chemistry; Regulatory Sequences, Nucleic Acid; RNA, Messenger - genetics; Sequence Alignment; Sequence Homology, Amino Acid; Transcription Factor MTF-1; Transcription Factors - chemistry; Transcription Factors - isolation & purification; Transcription Factors - metabolism

Metal responsive element (MRE) is a cis-acting DNA motif located in the upstream region of vertebrate metallothionein genes, which can confer metal responsiveness on downstream heterologous promoters. A protein that binds to the MRE sequence in a zinc-dependent manner (zinc regulatory factor; ZRF) w...