The MerR family of transcriptional regulators.
暂无分享,去创建一个
N. Brown | J. Hobman | S. Kidd | Jon L Hobman | Nigel L Brown | Jivko V. Stoyanov | Jivko V Stoyanov | Stephen P Kidd
[1] T. M. Bradley,et al. Binuclear [2Fe-2S] Clusters in the Escherichia coli SoxR Protein and Role of the Metal Centers in Transcription (*) , 1995, The Journal of Biological Chemistry.
[2] I. Lee,et al. The sctR of Salmonella enterica serova Typhimurium encoding a homologue of MerR protein is involved in the copper-responsive regulation of cuiD. , 2002, FEMS microbiology letters.
[3] N. Brown,et al. bacterial mercury-resistance genes. , 1997, Metal ions in biological systems.
[4] B. Demple,et al. Spacing of promoter elements regulates the basal expression of the soxS gene and converts SoxR from a transcriptional activator into a repressor , 1997, The EMBO journal.
[5] D. Gerhold,et al. The Bradyrhizobium japonicum nolA gene and its involvement in the genotype-specific nodulation of soybeans. , 1991, Proceedings of the National Academy of Sciences of the United States of America.
[6] Seon-Woo Lee,et al. Chromosomal Locus for Cadmium Resistance in Pseudomonas putida Consisting of a Cadmium-Transporting ATPase and a MerR Family Response Regulator , 2001, Applied and Environmental Microbiology.
[7] M. Mergeay,et al. Ralstonia metallidurans, a bacterium specifically adapted to toxic metals: towards a catalogue of metal-responsive genes. , 2003, FEMS microbiology reviews.
[8] N. Brown,et al. Transcriptional regulation of the mercury-resistance genes of transposon Tn501. , 1986, Journal of general microbiology.
[9] J. J. Díaz-Mejía,et al. Differential activities of the SoxR protein of Escherichia coli: SoxS is not required for gene activation under iron deprivation. , 2001, FEMS microbiology letters.
[10] C. Walsh,et al. Metalloregulatory DNA-binding protein encoded by the merR gene: isolation and characterization. , 1987, Science.
[11] Thomas V. O'Halloran,et al. De Novo Design of Mercury-Binding Two- and Three-Helical Bundles , 1997 .
[12] N. Brown,et al. Nucleotide sequence of a gene from the Pseudomonas transposon Tn501 encoding mercuric reductase. , 1983, Biochemistry.
[13] J. Lloyd,et al. Whole cell- and protein-based biosensors for the detection of bioavailable heavy metals in environmental samples , 1999 .
[14] D. Huffman,et al. Mercury-responsive gene regulation and mercury-199 as a probe of protein structure. , 1997, Metal ions in biological systems.
[15] B. Demple,et al. Redox signaling and gene control in the Escherichia coli soxRS oxidative stress regulon--a review. , 1996, Gene.
[16] C. Rensing,et al. CueO is a multi-copper oxidase that confers copper tolerance in Escherichia coli. , 2001, Biochemical and biophysical research communications.
[17] A. Heltzel,et al. Overexpression and DNA-binding properties of the mer-encoded regulatory protein from plasmid NR1 (Tn21) , 1987, Journal of bacteriology.
[18] M. Ahmed,et al. The drug-binding activity of the multidrug-responding transcriptional regulator BmrR resides in its C-terminal domain , 1996, Journal of bacteriology.
[19] M. R. Binet,et al. Cd(II), Pb(II) and Zn(II) ions regulate expression of the metal‐transporting P‐type ATPase ZntA in Escherichia coli , 2000, FEBS letters.
[20] J. Bryson,et al. Mercury-199 NMR of the metal receptor site in MerR and its protein-DNA complex. , 1995, Science.
[21] A. Odermatt,et al. Two trans-Acting Metalloregulatory Proteins Controlling Expression of the Copper-ATPases of Enterococcus hirae* , 1995, The Journal of Biological Chemistry.
[22] L. Møller,et al. Control of copper homeostasis in Escherichia coli by a P-type ATPase, CopA, and a MerR-like transcriptional activator, CopR. , 2000, Gene.
[23] A. Watson,et al. The Quality of merC, a Module of the mer Mosaic , 2000, Journal of Molecular Evolution.
[24] G. Nucifora,et al. Down regulation of the mercury resistance operon by the most promoter-distal gene merD , 1989, Molecular and General Genetics MGG.
[25] N. Brown,et al. The Escherichia coli Copper-responsivecopA Promoter Is Activated by Gold* , 2003, The Journal of Biological Chemistry.
[26] C. Walsh,et al. Transcriptional switching by the MerR protein: activation and repression mutants implicate distinct DNA and mercury(II) binding domains. , 1989, Biochemistry.
[27] L. Caslake,et al. Mutations in the alpha and sigma-70 subunits of RNA polymerase affect expression of the mer operon , 1997, Journal of bacteriology.
[28] J. Bradner,et al. DNA-bend modulation in a repressor-to-activator switching mechanism , 1995, Nature.
[29] A. Böck,et al. The hydH/G Genes from Escherichia coli code for a zinc and lead responsive two-component regulatory system. , 2001, Journal of molecular biology.
[30] N. Brown,et al. Cloning and Functional Analysis of thepbr Lead Resistance Determinant of Ralstonia metallidurans CH34 , 2001, Journal of bacteriology.
[31] R. A. Scott,et al. The core metal-recognition domain of MerR. , 1998, Biochemistry.
[32] M. Dilworth,et al. ActP controls copper homeostasis in Rhizobium leguminosarum bv. viciae and Sinorhizobium meliloti preventing low pH‐induced copper toxicity , 2002, Molecular microbiology.
[33] C. Walsh,et al. Mutagenesis of the cysteines in the metalloregulatory protein MerR indicates that a metal-bridged dimer activates transcription. , 1989, Biochemistry.
[34] S. Park,et al. Genetic analysis of the Tn21 mer operator-promoter , 1992, Journal of bacteriology.
[35] T. Foster,et al. Some mercurial resistance plasmids from different incompatibility groups specify merR regulatory functions that both repress and induce the mer operon of plasmid R100 , 1985, Journal of bacteriology.
[36] C. Walsh,et al. The MerR metalloregulatory protein binds mercuric ion as a tricoordinate, metal-bridged dimer. , 1990, Science.
[37] J. Altenbuchner,et al. Cloning and DNA sequence analysis of the mercury resistance genes of Streptomyces lividans , 1992, Molecular and General Genetics MGG.
[38] William R. Atchley,et al. Molecular Evolution of Helix–Turn–Helix Proteins , 1999, Journal of Molecular Evolution.
[39] M. Solioz,et al. Copper homeostasis in Enterococcus hirae. , 2003, FEMS microbiology reviews.
[40] D. Koshland. Switches, thresholds and ultrasensitivity , 1987 .
[41] K. Petrukhin,et al. Identification of a Novel Transcription Regulator from Proteus mirabilis, PMTR, Revealed a Possible Role of YJAI Protein in Balancing Zinc in Escherichia coli * , 1998, The Journal of Biological Chemistry.
[42] N. Brown,et al. The nucleotide sequence of the mercuric resistance operons of plasmid R100 and transposon Tn501: further evidence for mer genes which enhance the activity of the mercuric ion detoxification system , 2004, Molecular and General Genetics MGG.
[43] S. Taylor,et al. A protein that activates expression of a multidrug efflux transporter upon binding the transporter substrates. , 1994, The Journal of biological chemistry.
[44] B Demple,et al. Redox-operated genetic switches: the SoxR and OxyR transcription factors. , 2001, Trends in biotechnology.
[45] P. Bennett,et al. Characterization of a translocation unit encoding resistance to mercuric ions that occurs on a nonconjugative plasmid in Pseudomonas aeruginosa , 1977, Journal of bacteriology.
[46] A O Summers,et al. A mer-lux transcriptional fusion for real-time examination of in vivo gene expression kinetics and promoter response to altered superhelicity , 1992, Journal of bacteriology.
[47] R. Brennan,et al. Crystal structure of the transcription activator BmrR bound to DNA and a drug , 2001, Nature.
[48] K. Sharp,et al. The role of protonation and metal chelation preferences in defining the properties of mercury-binding coiled coils. , 1998, Journal of molecular biology.
[49] N. Brown,et al. Selection and characterization of mercury-independent activation mutants of the Tn501 transcriptional regulator, MerR. , 1998, Microbiology.
[50] G. Stacey,et al. Phenotypic characterization and regulation of the nolA gene of Bradyrhizobium japonicum. , 1996, Molecular plant-microbe interactions : MPMI.
[51] T. O’Halloran,et al. DNA Distortion Mechanism for Transcriptional Activation by ZntR, a Zn(II)-responsive MerR Homologue in Escherichia coli * , 1999, The Journal of Biological Chemistry.
[52] B Demple,et al. Two-stage control of an oxidative stress regulon: the Escherichia coli SoxR protein triggers redox-inducible expression of the soxS regulatory gene , 1992, Journal of bacteriology.
[53] A. Summers,et al. Translation of merD in Tn21 , 1989, Journal of bacteriology.
[54] C. Dozois,et al. MlrA, a novel regulator of curli (AgF) and extracellular matrix synthesis by Escherichia coli and Salmonella enterica serovar Typhimurium , 2001, Molecular microbiology.
[55] T. O’Halloran,et al. Ultrasensitivity and heavy-metal selectivity of the allosterically modulated MerR transcription complex. , 1990, Proceedings of the National Academy of Sciences of the United States of America.
[56] S. Taylor,et al. Two highly similar multidrug transporters of Bacillus subtilis whose expression is differentially regulated , 1995, Journal of bacteriology.
[57] J. Rutherford,et al. Cobalt-dependent Transcriptional Switching by a Dual-effector MerR-like Protein Regulates a Cobalt-exporting Variant CPx-type ATPase* , 1999, The Journal of Biological Chemistry.
[58] P. Griffin,et al. Characterization of the covalent binding of thiostrepton to a thiostrepton-induced protein from Streptomyces lividans. , 1996, Biochemistry.
[59] N. Brown,et al. Induction of bacterial mercury- and copper-responsive promoters: Functional differences between inducible systems and implications for their use in gene-fusions for in vivo metal biosensors , 1995, Journal of Industrial Microbiology.
[60] D. Mukhopadhyay,et al. Purification and functional characterization of MerD. A coregulator of the mercury resistance operon in gram-negative bacteria. , 1991, The Journal of biological chemistry.
[61] B. Demple,et al. An iron‐sulfur center essential for transcriptional activation by the redox‐sensing SoxR protein. , 1994, The EMBO journal.
[62] G. Stacey,et al. The Bradyrhizobium japonicum nolA Gene Encodes Three Functionally Distinct Proteins , 1999, Journal of bacteriology.
[63] S. Khan,et al. The functional analysis of directed amino-acid alterations in ZntR from Escherichia coli. , 2002, Biochemical and biophysical research communications.
[64] Nigel L. Brown,et al. Up-promoter mutations in the positively-regulated mer promoter of Tn501. , 1989, Nucleic acids research.
[65] A. Danchin,et al. Mta, a global MerR‐type regulator of the Bacillus subtilis multidrug‐efflux transporters , 1999, Molecular microbiology.
[66] B. Demple,et al. The redox‐regulated SoxR protein acts from a single DNA site as a repressor and an allosteric activator , 1998, The EMBO journal.
[67] T. O’Halloran,et al. Extreme zinc-binding thermodynamics of the metal sensor/regulator protein, ZntR. , 2001, Journal of the American Chemical Society.
[68] M. Buttner,et al. The bldC Developmental Locus of Streptomyces coelicolor Encodes a Member of a Family of Small DNA-Binding Proteins Related to the DNA-Binding Domains of the MerR Family , 2005, Journal of bacteriology.
[69] Susan M. Miller,et al. Bacterial mercury resistance from atoms to ecosystems. , 2003, FEMS microbiology reviews.
[70] Luis López-Maury,et al. A Gene Cluster Involved in Metal Homeostasis in the Cyanobacterium Synechocystis sp. Strain PCC 6803 , 2000, Journal of bacteriology.
[71] Soon-Jung Park,et al. In vivo DNA-protein interactions at the divergent mercury resistance (mer) promoters. II. Repressor/activator (MerR)-RNA polymerase interaction with merOP mutants. , 1993, Journal of Biological Chemistry.
[72] M. Merrick. A morphological and genetic mapping study of bald colony mutants of Streptomyces coelicolor. , 1976, Journal of general microbiology.
[73] B. Frantz,et al. The MerR heavy metal receptor mediates positive activation in a topologically novel transcription complex , 1989, Cell.
[74] R. Hall,et al. Transposon Tn21, Flagship of the Floating Genome , 1999, Microbiology and Molecular Biology Reviews.
[75] N. Brown,et al. Construction and characterization of a mercury‐independent MerR activator (MerRAC): transcriptional activation in the absence of Hg(II) is accompanied by DNA distortion. , 1993, The EMBO journal.
[76] The structure of the mer operon. , 1985, Basic life sciences.
[77] K. Comess,et al. Construction of a synthetic gene for the metalloregulatory protein MerR and analysis of regionally mutated proteins for transcriptional regulation. , 1994, Biochemistry.
[78] T. O’Halloran,et al. Coordination chemistry of the Hg-MerR metalloregulatory protein: evidence for a novel tridentate Hg-cysteine receptor site , 1990 .
[79] C. Thompson,et al. Autogenous transcriptional activation of a thiostrepton‐induced gene in Streptomyces lividans. , 1993, The EMBO journal.
[80] J. Hobman,et al. The sequence of the mer operon of pMER327/419 and transposon ends of pMER327/419, 330 and 05. , 1994, Gene.
[81] N. Brown,et al. Mercuric ion-resistance operons of plasmid R100 and transposon Tn501: the beginning of the operon including the regulatory region and the first two structural genes. , 1984, Proceedings of the National Academy of Sciences of the United States of America.
[82] A. Watson,et al. Cd(II)-Responsive and Constitutive Mutants Implicate a Novel Domain in MerR , 1999, Journal of bacteriology.
[83] A. Summers. Untwist and shout: a heavy metal-responsive transcriptional regulator , 1992, Journal of bacteriology.
[84] S. Swarup,et al. Molecular characterization of an operon, cueAR, encoding a putative P1-type ATPase and a MerR-type regulatory protein involved in copper homeostasis in Pseudomonas putida. , 2002, Microbiology.
[85] G. Stacey,et al. Nodulation Gene Regulation in Bradyrhizobium japonicum: a Unique Integration of Global Regulatory Circuits , 2003, Applied and Environmental Microbiology.
[86] S. Minakhina,et al. Mercury resistance transposons of gram-negative environmental bacteria and their classification. , 2001, Research in microbiology.
[87] N. Brown,et al. CueR (YbbI) of Escherichia coli is a MerR family regulator controlling expression of the copper exporter CopA , 2001, Molecular microbiology.
[88] T. White,et al. A merR homologue at 74 minutes on the Escherichia coli genome. , 1994, Gene.
[89] N. Brown,et al. ZntR is a Zn(II)‐responsive MerR‐like transcriptional regulator of zntA in Escherichia coli , 1999, Molecular microbiology.
[90] N. Brown,et al. Site-specific insertion and deletion mutants in the mer promoter-operator region of Tn501; the nineteen base-pair spacer is essential for normal induction of the promoter by MerR. , 1990, Nucleic acids research.
[91] C. Outten,et al. Femtomolar Sensitivity of Metalloregulatory Proteins Controlling Zinc Homeostasis , 2001, Science.
[92] S. J. Beard,et al. Zinc(II) tolerance in Escherichia coli K‐12: evidence that the zntA gene (o732) encodes a cation transport ATPase , 1997, Molecular microbiology.
[93] F. Murillo,et al. Role for Vitamin B12 in Light Induction of Gene Expression in the Bacterium Myxococcus xanthus , 2002, Journal of bacteriology.
[94] T. O’Halloran,et al. Transcriptional Activation of an Escherichia coliCopper Efflux Regulon by the Chromosomal MerR Homologue, CueR* , 2000, The Journal of Biological Chemistry.
[95] C. Thompson,et al. Ligand-induced changes in the Streptomyces lividans TipAL protein imply an alternative mechanism of transcriptional activation for MerR-like proteins. , 2001, Biochemistry.
[96] C. Vulpe,et al. CPx-type ATPases: a class of P-type ATPases that pump heavy metals. , 1996, Trends in biochemical sciences.
[97] J. Bryson,et al. Trigonal mercuric complex of an aliphatic thiolate: a spectroscopic and structural model for the receptor site in the Hg(II) biosensor MerR , 1990 .
[98] N. Brown,et al. ZccR--a MerR-like regulator from Bordetella pertussis which responds to zinc, cadmium, and cobalt. , 2003, Biochemical and biophysical research communications.
[99] J. Vohradský,et al. Broad Spectrum Thiopeptide Recognition Specificity of theStreptomyces lividans TipAL Protein and Its Role in Regulating Gene Expression* , 1999, The Journal of Biological Chemistry.
[100] R. Kulkarni,et al. MerR cross-links to the alpha, beta, and sigma 70 subunits of RNA polymerase in the preinitiation complex at the merTPCAD promoter. , 1999, Biochemistry.
[101] D. Koshland,et al. An amplified sensitivity arising from covalent modification in biological systems. , 1981, Proceedings of the National Academy of Sciences of the United States of America.
[102] G. Nucifora,et al. Mercury operon regulation by the merR gene of the organomercurial resistance system of plasmid pDU1358 , 1989, Journal of bacteriology.
[103] S. Park,et al. Genetic analysis of transcriptional activation and repression in the Tn21 mer operon , 1989, Journal of bacteriology.
[104] N. Brown,et al. Regulation of transcription in Escherichia coli from the mer and merR promoters in the transposon Tn501. , 1989, Journal of molecular biology.
[105] D. Giedroc,et al. The SmtB/ArsR family of metalloregulatory transcriptional repressors: Structural insights into prokaryotic metal resistance. , 2003, FEMS microbiology reviews.
[106] B. Demple,et al. Molecular characterization of the soxRS genes of Escherichia coli: two genes control a superoxide stress regulon. , 1991, Nucleic acids research.
[107] C. Walsh,et al. Homologous metalloregulatory proteins from both gram-positive and gram-negative bacteria control transcription of mercury resistance operons , 1989, Journal of bacteriology.
[108] Modification Between Zero-Order,et al. Ultrasensitivity in Biochemical Systems Controlled by Covalent , 1984 .
[109] A. Ansari,et al. Allosteric underwinding of DNA is a critical step in positive control of transcription by Hg-MerR , 1992, Nature.
[110] R. Brennan,et al. Crystal Structure of MtaN, a Global Multidrug Transporter Gene Activator* , 2001, The Journal of Biological Chemistry.
[111] S. Silver,et al. Nucleotide sequence and expression of the mercurial-resistance operon from Staphylococcus aureus plasmid pI258. , 1987, Proceedings of the National Academy of Sciences of the United States of America.
[112] W. Jackson,et al. The DNA sequence of the mercury resistance operon of the IncFII plasmid NR1. , 1984, Journal of molecular and applied genetics.
[113] T. M. Bradley,et al. Cysteine-to-alanine replacements in the Escherichia coli SoxR protein and the role of the [2Fe-2S] centers in transcriptional activation. , 1997, Nucleic acids research.
[114] A. Ishihama,et al. Protein-protein communication within the transcription apparatus , 1993, Journal of bacteriology.