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Frontispiece: C‐terminal Cysteines of CueR Act as Auxiliary Metal Site Ligands upon Hg II Binding—A Mechanism To Prevent Transcriptional Activation by Divalent Metal Ions?
Author(s) -
Balogh Ria K.,
Gyurcsik Béla,
HunyadiGulyás Éva,
Schell Juliana,
Thulstrup Peter W.,
Hemmingsen Lars,
Jancsó Attila
Publication year - 2019
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201986662
Subject(s) - divalent , transcription (linguistics) , binding site , metal , chemistry , transcriptional regulation , transcription factor , metal ions in aqueous solution , intracellular , divalent metal , stereochemistry , biophysics , regulator , biochemistry , crystallography , biology , gene , philosophy , linguistics , organic chemistry
The transcriptional regulator CueR controls the intracellular concentration of Cu I . Hg II exhibits strong binding to the bis‐thiolate functional metal binding site but does not induce transcription. Here it has been shown that HgS 3 structure appears under sub‐equimolar Hg II ‐concentrations at pH=8.0, suggesting that the conserved C‐terminal CCHH motif provides an auxiliary ligand for divalent metal ions, possibly preventing the transcription. For more information, see the Communication by A. Janscó et al. on page 15030 ff.