ArticleThe Journal of biological chemistry2009
Structural and functional analysis of SmeT, the repressor of the Stenotrophomonas maltophilia multidrug efflux pump SmeDEF.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed.
- Acquired resistance in Stenotrophomonas maltophilia: Mechanisms underlying the shift from multidrug to pandrug resistance.European journal of microbiology & immunology · 2026Review
- Designing modular genetic sensors with TtgR/AcrR family transcriptional regulators by using a statistical and data-driven approach.Nucleic acids research · 2025Article
- Versatility ofHeliyon · 2023Review
- What Approaches to Thwart Bacterial Efflux Pumps-Mediated Resistance?Antibiotics (Basel, Switzerland) · 2022Review
- Bacterial Multidrug Efflux Pumps at the Frontline of Antimicrobial Resistance: An Overview.Antibiotics (Basel, Switzerland) · 2022Review
- Evolution of cefiderocol resistance inJAC-antimicrobial resistance · 2022Article
- Polymerase Chain Reaction Assay for Detection of Stenotrophomonas maltophilia in Cheese Samples Based on the smeT Gene.Current microbiology · 2018Article
- Functional insights into the mode of DNA and ligand binding of the TetR family regulator TylP fromThe Journal of biological chemistry · 2017Article
- Article
- Crystallization and X-ray crystallographic analysis of recombinant TylP, a putative γ-butyrolactone receptor protein from Streptomyces fradiae.Acta crystallographica. Section F, Structural biology communications · 2017Article
- Bacterial Multidrug Efflux Pumps: Much More Than Antibiotic Resistance Determinants.Microorganisms · 2016Review
- Crystal structure of the Mycobacterium tuberculosis transcriptional regulator Rv0302.Protein science : a publication of the Protein Society · 2015Article
- Structural Basis for the Regulation of the MmpL Transporters of Mycobacterium tuberculosis.The Journal of biological chemistry · 2015Article
- Whole-genome sequencing identifies emergence of a quinolone resistance mutation in a case of Stenotrophomonas maltophilia bacteremia.Antimicrobial agents and chemotherapy · 2015Article
- The challenge of efflux-mediated antibiotic resistance in Gram-negative bacteria.Clinical microbiology reviews · 2015Review
- Update on infections caused by Stenotrophomonas maltophilia with particular attention to resistance mechanisms and therapeutic options.Frontiers in microbiology · 2015Review
- Article
- A function of SmeDEF, the major quinolone resistance determinant of Stenotrophomonas maltophilia, is the colonization of plant roots.Applied and environmental microbiology · 2014Article
- Clinical factors associated with acquisition of resistance to levofloxacin in Stenotrophomonas maltophilia.Yonsei medical journal · 2014Article
- Metabolic compensation of fitness costs associated with overexpression of the multidrug efflux pump MexEF-OprN in Pseudomonas aeruginosa.Antimicrobial agents and chemotherapy · 2014Article
Corrections and comments
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Authors and funding
6 authors.
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Abstract
Stenotrophomonas maltophilia is an opportunistic pathogen characterized for its intrinsic low susceptibility to several antibiotics. Part of this low susceptibility relies on the expression of chromosomally encoded multidrug efflux pumps, with SmeDEF being the most relevant antibiotic resistance efflux pump so far studied in this bacterial species. Expression of smeDEF is down-regulated by the SmeT repressor, encoded upstream smeDEF, in its complementary DNA strand. In the present article we present the crystal structure of SmeT and analyze its interactions with its cognate operator. Like other members of the TetR family of transcriptional repressors, SmeT behaves as a dimer and presents some common structural features with other TetR proteins like TtgR, QacR, and TetR. Differing from other TetR proteins for which the structure is available, SmeT turned out to have two extensions at the N and C termini that might be relevant for its function. Besides, SmeT presents the smallest binding pocket so far described in the TetR family of transcriptional repressors, which may correlate with a specific type and range of effectors. In vitro studies revealed that SmeT binds to a 28-bp pseudopalindromic region, forming two complexes. This operator region was found to overlap the promoters of smeT and smeDEF. This finding is consistent with a role for SmeT simultaneously down-regulating smeT and smeDEF transcription, likely by steric hindrance on RNA polymerase binding to DNA.
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