Frontispiece: C‐terminal Cysteines of CueR Act as Auxiliary Metal Site Ligands upon HgII Binding—A Mechanism To Prevent Transcriptional Activation by Divalent Metal Ions?

The transcriptional regulator CueR controls the intracellular concentration of CuI. HgII exhibits strong binding to the bis‐thiolate functional metal binding site but does not induce transcription. Here it has been shown that HgS3 structure appears under sub‐equimolar HgII‐concentrations at pH=8.0,...

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Veröffentlicht in:Chemistry : a European journal 2019-11, Vol.25 (66), p.n/a
Hauptverfasser: Balogh, Ria K., Gyurcsik, Béla, Hunyadi‐Gulyás, Éva, Schell, Juliana, Thulstrup, Peter W., Hemmingsen, Lars, Jancsó, Attila
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container_end_page n/a
container_issue 66
container_start_page
container_title Chemistry : a European journal
container_volume 25
creator Balogh, Ria K.
Gyurcsik, Béla
Hunyadi‐Gulyás, Éva
Schell, Juliana
Thulstrup, Peter W.
Hemmingsen, Lars
Jancsó, Attila
description The transcriptional regulator CueR controls the intracellular concentration of CuI. HgII exhibits strong binding to the bis‐thiolate functional metal binding site but does not induce transcription. Here it has been shown that HgS3 structure appears under sub‐equimolar HgII‐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.
doi_str_mv 10.1002/chem.201986662
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subjects Binding sites
Chemistry
coordination modes
CueR metalloregulatory protein
Ions
Ligands
mercury
metal ion selectivity
Metal ions
perturbed angular correlation (PAC) spectroscopy
Transcription activation
title Frontispiece: C‐terminal Cysteines of CueR Act as Auxiliary Metal Site Ligands upon HgII Binding—A Mechanism To Prevent Transcriptional Activation by Divalent Metal Ions?
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