scholarly journals Structural and biochemical characterization of MepR, a multidrug binding transcription regulator of the Staphylococcus aureus multidrug efflux pump MepA

2009 ◽  
Vol 37 (4) ◽  
pp. 1211-1224 ◽  
Author(s):  
Muthiah Kumaraswami ◽  
Jason T. Schuman ◽  
Susan M. Seo ◽  
Glenn W. Kaatz ◽  
Richard G. Brennan
Keyword(s):  
Staphylococcus Aureus ◽  
Biochemical Characterization ◽  
Efflux Pump ◽  
Multidrug Efflux ◽  
Multidrug Efflux Pump ◽  
Transcription Regulator

scholarly journals Functional Gene Cloning and Characterization of MdeA, a Multidrug Efflux Pump from Staphylococcus aureus

2006 ◽  
Vol 29 (4) ◽  
pp. 801-804 ◽  
Author(s):  
Youichi Yamada ◽  
Sumiko Shiota ◽  
Tohru Mizushima ◽  
Teruo Kuroda ◽  
Tomofusa Tsuchiya
Keyword(s):  
Staphylococcus Aureus ◽  
Gene Cloning ◽  
Efflux Pump ◽  
Functional Gene ◽  
Multidrug Efflux ◽  
Multidrug Efflux Pump ◽  
Gene Cloning And Characterization

scholarly journals Gene Cloning and Characterization of SdrM, a Chromosomally-Encoded Multidrug Efflux Pump, from Staphylococcus aureus

2006 ◽  
Vol 29 (3) ◽  
pp. 554-556 ◽  
Author(s):  
Youichi Yamada ◽  
Koh-ichiro Hideka ◽  
Sumiko Shiota ◽  
Teruo Kuroda ◽  
Tomofusa Tsuchiya
Keyword(s):  
Staphylococcus Aureus ◽  
Gene Cloning ◽  
Efflux Pump ◽  
Multidrug Efflux ◽  
Multidrug Efflux Pump ◽  
Gene Cloning And Characterization

scholarly journals Gene Cloning and Characterization of VcrM, a Na+-Coupled Multidrug Efflux Pump, fromVibrio choleraeNon-O1

2003 ◽  
Vol 47 (6) ◽  
pp. 419-427 ◽  
Author(s):  
Md. Nazmul Huda ◽  
Jing Chen ◽  
Yuji Morita ◽  
Teruo Kuroda ◽  
Tohru Mizushima ◽  
...  
Keyword(s):  
Gene Cloning ◽  
Efflux Pump ◽  
Multidrug Efflux ◽  
Multidrug Efflux Pump ◽  
Gene Cloning And Characterization

scholarly journals Cloning and Characterization of SmeT, a Repressor of the Stenotrophomonas maltophilia Multidrug Efflux Pump SmeDEF

2002 ◽  
Vol 46 (11) ◽  
pp. 3386-3393 ◽  
Author(s):  
Patricia Sánchez ◽  
Ana Alonso ◽  
Jose L. Martinez
Keyword(s):  
Stenotrophomonas Maltophilia ◽  
Efflux Pump ◽  
Wild Type ◽  
Multidrug Efflux ◽  
Multidrug Efflux Pump ◽  
S1 Nuclease ◽  
Cellular Factor ◽  
S1 Nuclease Mapping ◽  
Nuclease Mapping

ABSTRACT We report on the cloning of the gene smeT, which encodes the transcriptional regulator of the Stenotrophomonas maltophilia efflux pump SmeDEF. SmeT belongs to the TetR and AcrR family of transcriptional regulators. The smeT gene is located upstream from the structural operon of the pump genes smeDEF and is divergently transcribed from those genes. Experiments with S. maltophilia and the heterologous host Escherichia coli have demonstrated that SmeT is a transcriptional repressor. S1 nuclease mapping has demonstrated that expression of smeT is driven by a single promoter lying close to the 5′ end of the gene and that expression of smeDEF is driven by an unique promoter that overlaps with promoter PsmeT. The level of expression of smeT is higher in smeDEF-overproducing S. maltophilia strain D457R, which suggests that SmeT represses its own expression. Band-shifting assays have shown that wild-type strain S. maltophilia D457 contains a cellular factor(s) capable of binding to the intergenic smeT-smeD region. That cellular factor(s) was absent from smeDEF-overproducing S. maltophilia strain D457R. The sequence of smeT from D457R showed a point mutation that led to a Leu166Gln change within the SmeT protein. This change allowed overexpression of both smeDEF and smeT in D457R. It was noteworthy that expression of wild-type SmeT did not fully complement the smeT mutation in D457R. This suggests that the wild-type protein is not dominant over the mutant SmeT.

scholarly journals Response of Staphylococcus aureus to Salicylate Challenge

2006 ◽  
Vol 189 (1) ◽  
pp. 220-227 ◽  
Author(s):  
James T. Riordan ◽  
Arunachalam Muthaiyan ◽  
Wayne Van Voorhies ◽  
Christopher T. Price ◽  
James E. Graham ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Antimicrobial Resistance ◽  
Transcriptome Analysis ◽  
Target Genes ◽  
Efflux Pump ◽  
Multidrug Efflux ◽  
Multidrug Efflux Pump ◽  
Antibiotic Target ◽  
Unique Mechanism ◽  
Formate Metabolism

ABSTRACT Growth of Staphylococcus aureus with the nonsteroidal anti-inflammatory salicylate reduces susceptibility of the organism to multiple antimicrobials. Transcriptome analysis revealed that growth of S. aureus with salicylate leads to the induction of genes involved with gluconate and formate metabolism and represses genes required for gluconeogenesis and glycolysis. In addition, salicylate induction upregulates two antibiotic target genes and downregulates a multidrug efflux pump gene repressor (mgrA) and sarR, which represses a gene (sarA) important for intrinsic antimicrobial resistance. We hypothesize that these salicylate-induced alterations jointly represent a unique mechanism that allows S. aureus to resist antimicrobial stress and toxicity.

Characterization of the Serratia marcescens SdeCDE multidrug efflux pump studied via gene knockout mutagenesis

2008 ◽  
Vol 54 (5) ◽  
pp. 411-416 ◽  
Author(s):  
Sanela Begic ◽  
Elizabeth A. Worobec
Keyword(s):  
Antibiotic Resistance ◽  
Substrate Specificity ◽  
Serratia Marcescens ◽  
Efflux Pump ◽  
Gene Knockout ◽  
Multidrug Efflux ◽  
Multidrug Efflux Pump ◽  
Active Efflux ◽  
Major Mechanism

Serratia marcescens is an important nosocomial agent having high antibiotic resistance. A major mechanism for S. marcescens antibiotic resistance is active efflux. To ascertain the substrate specificity of the S. marcescens SdeCDE efflux pump, we constructed pump gene deletion mutants. sdeCDE knockout strains showed no change in antibiotic susceptibility in comparison with the parental strains for any of the substrates, with the exception of novobiocin. In addition, novobiocin was the only antibiotic to be accumulated by sdeCDE-deficient strains. Based on the substrates used in our study, we conclude that SdeCDE is a Resistance–Nodulation–Cell Division family pump with limited substrate specificity.

scholarly journals Molecular Cloning and Characterization of the HmrM Multidrug Efflux Pump fromHaemophilus influenzaeRd

2003 ◽  
Vol 47 (12) ◽  
pp. 937-943 ◽  
Author(s):  
Xing-Jue Xu ◽  
Xian-Zhong Su ◽  
Yuji Morita ◽  
Teruo Kuroda ◽  
Tohru Mizushima ◽  
...  
Keyword(s):  
Molecular Cloning ◽  
Efflux Pump ◽  
Multidrug Efflux ◽  
Multidrug Efflux Pump

scholarly journals Functional Cloning and Characterization of a Multidrug Efflux Pump, MexHI-OpmD, from a Pseudomonas aeruginosa Mutant

2003 ◽  
Vol 47 (9) ◽  
pp. 2990-2992 ◽  
Author(s):  
Hiroshi Sekiya ◽  
Takehiko Mima ◽  
Yuji Morita ◽  
Teruo Kuroda ◽  
Tohru Mizushima ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Ethidium Bromide ◽  
Rhodamine 6G ◽  
Efflux Pump ◽  
Efflux Pumps ◽  
Multidrug Efflux ◽  
Chromosomal Dna ◽  
Multidrug Efflux Pump ◽  
Multidrug Efflux Pumps

ABSTRACT We isolated mutant YM644, which showed elevated resistance to norfloxacin, ethidium bromide, acriflavine, and rhodamine 6G, from Pseudomonas aeruginosa YM64, a strain that lacks four major multidrug efflux pumps. The genes responsible for the resistance were mexHI-opmD. Elevated ethidium extrusion was observed with cells of YM644 and YM64 harboring a plasmid carrying the genes. Disruption of the genes in the chromosomal DNA of YM644 made the cells sensitive to the drugs.

scholarly journals MepR, a Repressor of the Staphylococcus aureus MATE Family Multidrug Efflux Pump MepA, Is a Substrate-Responsive Regulatory Protein

2006 ◽  
Vol 50 (4) ◽  
pp. 1276-1281 ◽  
Author(s):  
Glenn W. Kaatz ◽  
Carmen E. DeMarco ◽  
Susan M. Seo
Keyword(s):  
Staphylococcus Aureus ◽  
Efflux Pump ◽  
Regulatory Protein ◽  
Inducible Promoter ◽  
Multidrug Efflux ◽  
Recognition Sequence ◽  
Multidrug Efflux Pump ◽  
Mobility Shift ◽  
Repressive Effect ◽  
Operator Interaction

ABSTRACT The mepRAB gene cluster of Staphylococcus aureus encodes a MarR family repressor (MepR; known to repress mepA expression), a MATE family multidrug efflux pump (MepA), and a protein of unknown function (MepB). In this report, we show that MepR also is autoregulatory, repressing the expression of its own gene. Exposure of strains containing a mepR::lacZ fusion with mepR provided in trans under the control of an inducible promoter, or a mepA::lacZ fusion alone, to subinhibitory concentrations of MepA substrates resulted in variably increased expression mainly of mepA. Mobility shift assays revealed that MepR binds upstream of mepR and mepA, with an apparently higher affinity for the mepA binding site. MepA substrates abrogated MepR binding to each site in a differential manner, with the greatest effect observed on the MepR-mepA operator interaction. DNase I footprinting identified precise binding sites which included promoter motifs, inverted repeats, and transcription start sites for mepR and mepA, as well as a conserved GTTAG motif, which may be a signature recognition sequence for MepR. Analogous to other multidrug efflux pump regulatory proteins such as QacR, the substrate-MepR interaction likely results in its dissociation from its mepA, and in a more limited fashion its mepR, operator sites and relief of its repressive effect. The enhanced effect of substrates on mepA compared to mepR expression, and on the MepR-mepA operator interaction, results in significant relief of mepA and relative maintenance of mepR repression, leading to increased MepA protein unimpeded by MepR when the need for detoxification exists.

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