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 |
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container_title | Chemistry : a European journal |
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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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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. 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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.</description><subject>Binding sites</subject><subject>Chemistry</subject><subject>coordination modes</subject><subject>CueR metalloregulatory protein</subject><subject>Ions</subject><subject>Ligands</subject><subject>mercury</subject><subject>metal ion selectivity</subject><subject>Metal ions</subject><subject>perturbed angular correlation (PAC) spectroscopy</subject><subject>Transcription activation</subject><issn>0947-6539</issn><issn>1521-3765</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><recordid>eNo9kc1u1DAUhS0EEkPLlvWVWKf4J3FsNmgILTPSVFRlWEdOcjN1lXGC7RRm10dg0efoQ_VJmmhQV_ce6dM5V_cQ8oHRM0Yp_1Tf4P6MU6aVlJK_IguWcZaIXGavyYLqNE9kJvRb8i6EW0qplkIsyOOF7120YbBY42conu7_RfR760wHxSFEtA4D9C0UI17Dso5gAizHv7azxh_gEuME_rQRYWN3xjUBxqF3sNqt1_DVusa63dP9w3IC6xvjbNjDtocrj3foImy9caH2doi2nwMne3tnZgHVAb5Nezdjx5B178KXU_KmNV3A9__nCfl1cb4tVsnmx_d1sdwkA2OKJ7nIldZpbURT05aiqlJhuOSqUVg3WU6bSmgts0oKNFRXmNEKVcaVaHOdtpU4IR-PvoPvf48YYnnbj366MZRcMJUrkSo5UfpI_bEdHsrB2_30lJLRci6knAspXwopi9X55YsSzxsihYA</recordid><startdate>20191127</startdate><enddate>20191127</enddate><creator>Balogh, Ria K.</creator><creator>Gyurcsik, Béla</creator><creator>Hunyadi‐Gulyás, Éva</creator><creator>Schell, Juliana</creator><creator>Thulstrup, Peter W.</creator><creator>Hemmingsen, Lars</creator><creator>Jancsó, Attila</creator><general>Wiley Subscription Services, Inc</general><scope>7SR</scope><scope>8BQ</scope><scope>8FD</scope><scope>JG9</scope><scope>K9.</scope><orcidid>https://orcid.org/0000-0002-1823-3035</orcidid><orcidid>https://orcid.org/0000-0003-2362-0758</orcidid></search><sort><creationdate>20191127</creationdate><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?</title><author>Balogh, Ria K. ; Gyurcsik, Béla ; Hunyadi‐Gulyás, Éva ; Schell, Juliana ; Thulstrup, Peter W. ; Hemmingsen, Lars ; Jancsó, Attila</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p1182-7378994ca3dc0f0e8b43a2628d8ecd570db39965b63ea09be50be85283f794fb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>Binding sites</topic><topic>Chemistry</topic><topic>coordination modes</topic><topic>CueR metalloregulatory protein</topic><topic>Ions</topic><topic>Ligands</topic><topic>mercury</topic><topic>metal ion selectivity</topic><topic>Metal ions</topic><topic>perturbed angular correlation (PAC) spectroscopy</topic><topic>Transcription activation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Balogh, Ria K.</creatorcontrib><creatorcontrib>Gyurcsik, Béla</creatorcontrib><creatorcontrib>Hunyadi‐Gulyás, Éva</creatorcontrib><creatorcontrib>Schell, Juliana</creatorcontrib><creatorcontrib>Thulstrup, Peter W.</creatorcontrib><creatorcontrib>Hemmingsen, Lars</creatorcontrib><creatorcontrib>Jancsó, Attila</creatorcontrib><collection>Engineered Materials Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Materials Research Database</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><jtitle>Chemistry : a European journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Balogh, Ria K.</au><au>Gyurcsik, Béla</au><au>Hunyadi‐Gulyás, Éva</au><au>Schell, Juliana</au><au>Thulstrup, Peter W.</au><au>Hemmingsen, Lars</au><au>Jancsó, Attila</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>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?</atitle><jtitle>Chemistry : a European journal</jtitle><date>2019-11-27</date><risdate>2019</risdate><volume>25</volume><issue>66</issue><epage>n/a</epage><issn>0947-6539</issn><eissn>1521-3765</eissn><abstract>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.</abstract><cop>Weinheim</cop><pub>Wiley Subscription Services, Inc</pub><doi>10.1002/chem.201986662</doi><tpages>1</tpages><orcidid>https://orcid.org/0000-0002-1823-3035</orcidid><orcidid>https://orcid.org/0000-0003-2362-0758</orcidid><oa>free_for_read</oa></addata></record> |
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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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