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Thionein (apometallothionein) can modulate DNA binding and transcription activation by zinc finger containing factor Spl
Author(s) -
Zeng Jin,
Heuchel Rainer,
Schaffner Walter,
Kägi Jeremias H.R.
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80175-3
Subject(s) - zinc finger , transcription factor , sp1 transcription factor , transcription (linguistics) , dna binding protein , dna , zinc , dna binding domain , chemistry , zinc finger transcription factor , zinc finger nuclease , microbiology and biotechnology , biochemistry , biology , gene , promoter , gene expression , organic chemistry , linguistics , philosophy
A number of transcription factors contain so‐called zinc finger domains for the interaction with their cognate DNA sequence. It has been shown that removal of the zinc ions complexed in these zinc fingers abrogates DNA binding and transcription activation. Therefore we wanted to test the hypothesis that the activity of transcription factors could be regulated by physiological chelators of zinc. A prominent candidate for such a chelator is the Cys‐rich protein thionein (apometallothionein) that is inducible by heavy metal loads, and by other environmental stimuli. Here we show with DNA binding and in vitro transcriptions assays that thionein indeed can inactive the zinc finger‐containing Spl in a reversible manner. By contrast, transcription factor Oct‐l, which binds DNA via a homeo‐domain, i.e. a helix‐turn‐helix motif not involving zinc ions, is refractory to thionein action. We propose that modulation of intracellular thionein concentration is used for the coordinated regulation of a large subset of genes whose transcription depends on zinc finger proteins.