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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Nuclear receptor binding factor 2

CopR, COPR1, comodulator of PPAR and RXR, COPR2
Top mentioned proteins: ACID, CopA, ATPase, CAN, beta-COP
Papers on CopR
Antisense-RNA mediated control of plasmid replication - pIP501 revisited.
Brantl, Jena, Germany. In Plasmid, Mar 2015
Plasmid pIP501 uses two copy number-control elements, RNAIII, a cis-encoded antisense RNA, and transcriptional repressor CopR.
CopM is a novel copper-binding protein involved in copper resistance in Synechocystis sp. PCC 6803.
Florencio et al., Sevilla, Spain. In Microbiologyopen, Feb 2015
Moreover, constitutive expression of copM is able to partially suppress the copper sensitivity of the copR mutant strain, pointing out that CopM per se is able to confer copper resistance.
A copper-induced quinone degradation pathway provides protection against combined copper/quinone stress in Lactococcus lactis IL1403.
Solioz et al., Bern, Switzerland. In Mol Microbiol, Feb 2015
The operon is under the control of CopR, which also regulates expression of the copRZA copper resistance operon as well as other L. lactis genes.
Characterization and structure prediction of partial length protein sequences of pcoA, pcoR and chrB genes from heavy metal resistant bacteria from the Klip River, South Africa.
Pillay et al., Vanderbijlpark, South Africa. In Int J Mol Sci, 2014
Open reading frames (ORFs) related to the genes CopA and CopR were identified in E. coli KR29, PcoA in Lysinibacillus sp.
Global transcriptional profiles of the copper responses in the cyanobacterium Synechocystis sp. PCC 6803.
Florencio et al., Sevilla, Spain. In Plos One, 2013
Here, we report the transcriptional responses to copper additions at non-toxic (0.3 µM) and toxic concentrations (3 µM) in the wild type and in the copper sensitive copR mutant strain.
Metal resistance and lithoautotrophy in the extreme thermoacidophile Metallosphaera sedula.
Blum et al., Lincoln, United States. In J Bacteriol, 2012
The functional role of the M. sedula copRTA operon was demonstrated by cross-species complementation of a copper-sensitive Sulfolobus solfataricus copR mutant.
The heavy metal tolerant soil bacterium Achromobacter sp. AO22 contains a unique copper homeostasis locus and two mer operons.
Bhave et al., Melbourne, Australia. In J Microbiol Biotechnol, 2012
CopA, B, C, and D exhibit several potential copper ligands and CopS and CopR exhibit features of two-component regulatory systems.
Identification of a copper-responsive promoter and development of a copper biosensor in the soil bacterium Achromobacter sp. AO22.
Bhave et al., Melbourne, Australia. In World J Microbiol Biotechnol, 2012
A section located between the divergently transcribed putative response regulator gene copR and multicopper oxidase gene copA that included a palindromic cop box was identified as a copper-responsive promoter using a lacZ reporter construct, pCOPRP, in E. coli.
CopR of Sulfolobus solfataricus represents a novel class of archaeal-specific copper-responsive activators of transcription.
Bini et al., New Brunswick, United States. In Microbiology, 2011
Here we show that the Sulfolobus CopR represents a novel class of copper-responsive regulators, unique to the archaeal domain.
Transcriptional repressor CopR acts by inhibiting RNA polymerase binding.
Brantl et al., Jena, Germany. In Microbiology, 2011
CopR is a transcriptional repressor encoded by the broad-host-range streptococcal plasmid pIP501, which also replicates in Bacillus subtilis.
Regulation and structure of YahD, a copper-inducible α/β serine hydrolase of Lactococcus lactis IL1403.
Solioz et al., Berlin, Germany. In Fems Microbiol Lett, 2011
This enzyme is under the control of the CopR transcriptional regulator.
The two-component signal transduction system CopRS of Corynebacterium glutamicum is required for adaptation to copper-excess stress.
Brocker et al., Jülich, Germany. In Plos One, 2010
In addition, this region includes the copRS genes (previously named cgtRS9) which encode a two-component signal transduction system composed of the histidine kinase CopS and the response regulator CopR.
Functional and expression analyses of the cop operon, required for copper resistance in Agrobacterium tumefaciens.
Vattanaviboon et al., Bangkok, Thailand. In J Bacteriol, 2009
These genes are transcribed as an operon, and their expression is induced in response to increasing copper and silver ion concentrations in a copR-dependent fashion.
Molecular analysis of the copper-responsive CopRSCD of a pathogenic Pseudomonas fluorescens strain.
Sun et al., Qingdao, China. In J Microbiol, 2009
In this study a genetic cluster, consisting of copR, S, C, and D but lacking copAB, was identified in a pathogenic P. fluorescens strain (TSS) isolated from diseased fish.
Corepressors of agonist-bound nuclear receptors.
Aneskievich et al., United States. In Toxicol Appl Pharmacol, 2007
Among them are LCoR, PRAME, REA, MTA1, NSD1, and COPR1 Although they exhibit a great diversity of structure, mechanism of repression and pathophysiological function, these corepressors frequently have one or more NR boxes and often recruit histone deacetylases to exert their repressive effects.
Isolation and functional analysis of a keratinocyte-derived, ligand-regulated nuclear receptor comodulator.
Aneskievich et al., United States. In J Invest Dermatol, 2004
The activation domain, their small size (COPR1, 26.9 kDa; COPR2, 32.4 kDa), and strict dependence on AF-2 for interaction distinguish COPR1 and COPR2 from the SMRT/NCoR type of corepressor and may dampen rather than repress NR-mediated gene expression.
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