Publication:
The copper-inducible ComR (YcfQ) repressor regulates expression of ComC (YcfR), which affects copper permeability of the outer membrane of Escherichia coli

cris.virtual.author-orcid#PLACEHOLDER_PARENT_METADATA_VALUE#
cris.virtual.author-orcid#PLACEHOLDER_PARENT_METADATA_VALUE#
cris.virtual.author-orcid#PLACEHOLDER_PARENT_METADATA_VALUE#
cris.virtual.author-orcid#PLACEHOLDER_PARENT_METADATA_VALUE#
cris.virtualsource.author-orcid#PLACEHOLDER_PARENT_METADATA_VALUE#
cris.virtualsource.author-orcid#PLACEHOLDER_PARENT_METADATA_VALUE#
cris.virtualsource.author-orcidd8950f41-1d28-4203-a2f6-c51aeb0d9760
cris.virtualsource.author-orcid#PLACEHOLDER_PARENT_METADATA_VALUE#
dc.contributor.authorMermod, Mélanie
dc.contributor.authorMagnani, David
dc.contributor.authorSolioz, Marc
dc.contributor.authorStoyanov, Jivko V
dc.date.accessioned2024-10-11T09:26:50Z
dc.date.available2024-10-11T09:26:50Z
dc.date.issued2012
dc.description.abstractThe pathway of copper entry into Escherichia coli is still unknown. In an attempt to shed light on this process, a lux-based biosensor was utilized to monitor intracellular copper levels in situ. From a transposon-mutagenized library, strains were selected in which copper entry into cells was reduced, apparent as clones with reduced luminescence when grown in the presence of copper (low-glowers). One low-glower had a transposon insertion in the comR gene, which encodes a TetR-like transcriptional regulator. The mutant strain could be complemented by the comR gene on a plasmid, restoring luminescence to wild-type levels. ComR did not regulate its own expression, but was required for copper-induction of the neighboring, divergently transcribed comC gene, as shown by real-time quantitative PCR and with a promoter-lux fusion. The purified ComR regulator bound to the promoter region of the comC gene in vitro and was released by copper. By membrane fractionation, ComC was shown to be localized in the outer membrane. When grown in the presence of copper, ∆comC cells had higher periplasmic and cytoplasmic copper levels, compared to the wild-type, as assessed by the activation of the periplasmic CusRS sensor and the cytoplasmic CueR sensor, respectively. Thus, ComC is an outer membrane protein which lowers the permeability of the outer membrane to copper. The expression of ComC is controlled by ComR, a novel, TetR-like copper-responsive repressor.
dc.description.numberOfPages11
dc.description.sponsorshipDepartement Klinische Forschung, Hepatologie Forschung
dc.identifier.doi10.7892/boris.7742
dc.identifier.isi000299485000004
dc.identifier.pmid22089859
dc.identifier.publisherDOI10.1007/s10534-011-9510-x
dc.identifier.urihttps://boris-portal.unibe.ch/handle/20.500.12422/78193
dc.language.isoen
dc.publisherSpringer Netherlands
dc.publisher.placeOxford
dc.relation.ispartofBioMetals
dc.relation.issn0966-0844
dc.relation.organizationDCD5A442BBC5E17DE0405C82790C4DE2
dc.titleThe copper-inducible ComR (YcfQ) repressor regulates expression of ComC (YcfR), which affects copper permeability of the outer membrane of Escherichia coli
dc.typearticle
dspace.entity.typePublication
dspace.file.typetext
oaire.citation.endPage43
oaire.citation.issue1
oaire.citation.startPage33
oaire.citation.volume25
oairecerif.author.affiliation#PLACEHOLDER_PARENT_METADATA_VALUE#
oairecerif.author.affiliation#PLACEHOLDER_PARENT_METADATA_VALUE#
oairecerif.author.affiliationDepartement Klinische Forschung, Hepatologie Forschung
oairecerif.author.affiliation#PLACEHOLDER_PARENT_METADATA_VALUE#
oairecerif.author.affiliation2#PLACEHOLDER_PARENT_METADATA_VALUE#
oairecerif.author.affiliation2#PLACEHOLDER_PARENT_METADATA_VALUE#
oairecerif.author.affiliation2#PLACEHOLDER_PARENT_METADATA_VALUE#
oairecerif.author.affiliation2#PLACEHOLDER_PARENT_METADATA_VALUE#
oairecerif.author.affiliation3#PLACEHOLDER_PARENT_METADATA_VALUE#
oairecerif.author.affiliation3#PLACEHOLDER_PARENT_METADATA_VALUE#
oairecerif.author.affiliation3#PLACEHOLDER_PARENT_METADATA_VALUE#
oairecerif.author.affiliation3#PLACEHOLDER_PARENT_METADATA_VALUE#
oairecerif.author.affiliation4#PLACEHOLDER_PARENT_METADATA_VALUE#
oairecerif.author.affiliation4#PLACEHOLDER_PARENT_METADATA_VALUE#
oairecerif.author.affiliation4#PLACEHOLDER_PARENT_METADATA_VALUE#
oairecerif.author.affiliation4#PLACEHOLDER_PARENT_METADATA_VALUE#
unibe.contributor.rolecreator
unibe.contributor.rolecreator
unibe.contributor.rolecreator
unibe.contributor.rolecreator
unibe.date.licenseChanged2019-10-24 18:59:33
unibe.description.ispublishedpub
unibe.eprints.legacyId7742
unibe.journal.abbrevTitleBIOMETALS
unibe.refereedTRUE
unibe.subtype.articlejournal

Files

Original bundle
Now showing 1 - 1 of 1
Name:
10534_2011_Article_9510.pdf
Size:
498.83 KB
Format:
Adobe Portable Document Format
File Type:
text
License:
publisher
Content:
published

Collections