Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Functional consequences of substitution mutations in MepR, a repressor of the Staphylococcus aureus MepA multidrug efflux pump gene.

Journal of bacteriology - 1 Aug 2013

Schindler Bryan D, Seo Susan M, Jacinto Pauline L, Kumaraswami Muthiah, Birukou Ivan, Brennan Richard G, Kaatz Glenn W

Abstract excerpt

The expression of mepA, encoding the Staphylococcus aureus MepA multidrug efflux protein, is repressed by the MarR homologue MepR. MepR dimers bind differently to operators upstream of mepR and mepA, with affinity being greatest at the mepA operator. MepR substitution mutations may result in mepA overexpression, with A103V most common in clinical strains. Evaluation of the functional consequences of this and...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Substitution
Share to Anti-Bacterial Agents

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Drug Resistance, Multiple, Bacterial

Share to Gene Expression Regulation, Bacterial

Share to Genes, MDR

Share to Protein Conformation

Share to Reverse Transcriptase Polymerase Chain Reaction

Share to Staphylococcus aureus

Source

Open in PubMed Open full text

Identifiers

PMID: 23749979
DOI: 10.1128/JB.00565-13
PMCID: PMC3754585

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Functional consequences of substitution mutations in MepR, a repressor of the Staphylococcus aureus MepA multidrug efflux pump gene.PMID 23749979Read ↗

Mutations within the mepA operator affect binding of the MepR regulatory protein and its induction by MepA substrates in Staphylococcus aureus.Semantic proximity Read ↗

Structural and biochemical characterization of MepR, a multidrug binding transcription regulator of the Staphylococcus aureus multidrug efflux pump MepA.Semantic proximity Read ↗

The mexR repressor of the mexAB-oprM multidrug efflux operon in Pseudomonas aeruginosa: characterization of mutations compromising activity.Semantic proximity Read ↗

Structure and function of the macrolide biosensor protein, MphR(A), with and without erythromycin.Semantic proximity Read ↗

Multidrug resistance in Staphylococcus aureus due to overexpression of a novel multidrug and toxin extrusion (MATE) transport protein.Semantic proximity Read ↗

Role of a conserved residue R780 in Escherichia coli multidrug transporter AcrB.Semantic proximity Read ↗

Protein modulator of multidrug efflux gene expression in Pseudomonas aeruginosa.Semantic proximity Read ↗

Effect of promoter region mutations and mgrA overexpression on transcription of norA, which encodes a Staphylococcus aureus multidrug efflux transporter.Semantic proximity Read ↗

Efflux-mediated bis-indole resistance in Staphylococcus aureus reveals differential substrate specificities for MepA and MepR.Semantic proximity Read ↗

Critical biophysical properties in the Pseudomonas aeruginosa efflux gene regulator MexR are targeted by mutations conferring multidrug resistance.Semantic proximity Read ↗

Characterization of NorR protein, a multifunctional regulator of norA expression in Staphylococcus aureus.Semantic proximity Read ↗

Development of Genetically Encoded Biosensors for Reporting the Methyltransferase-Dependent Biosynthesis of Semisynthetic Macrolide AntibioticsSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.