ArticleBiochemistry2003
TetL tetracycline efflux protein from Bacillus subtilis is a dimer in the membrane and in detergent solution.
Article in Biochemistry, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 25 citations in OpenAlex.
- Genomic Characterization ofFrontiers in microbiology · 2022Article
- Agricultural Origins of a Highly Persistent Lineage of Vancomycin-ResistantApplied and environmental microbiology · 2019Article
- Rapid Bioinformatic Identification of Thermostabilizing Mutations.Biophysical journal · 2015Article
- The Structure and Function of OxlT, the Oxalate Transporter of Oxalobacter formigenes.The Journal of membrane biology · 2015Review
- Molecular Mechanism Underlying the Plant NRT1.1 Dual-Affinity Nitrate Transporter.Frontiers in physiology · 2015Review
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- Oligomeric state of the oxalate transporter, OxlT.Biochemistry · 2011Article
- Review
- Modulation of Bacillus thuringiensis phosphatidylinositol-specific phospholipase C activity by mutations in the putative dimerization interface.The Journal of biological chemistry · 2009Article
- The Vibrio cholerae Mrp system: cation/proton antiport properties and enhancement of bile salt resistance in a heterologous host.Journal of molecular microbiology and biotechnology · 2009Article
- Ins and outs of major facilitator superfamily antiporters.Annual review of microbiology · 2008Review
- Catalytic properties of Staphylococcus aureus and Bacillus members of the secondary cation/proton antiporter-3 (Mrp) family are revealed by an optimized assay in an Escherichia coli host.Journal of bacteriology · 2007Article
- The Mrp system: a giant among monovalent cation/proton antiporters?Extremophiles : life under extreme conditions · 2005Review
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
The TetL antiporter from the Bacillus subtilis inner membrane is a tetracycline-divalent cation efflux protein that is energized by the electrochemical proton gradient across the membrane. In this study, we expressed tetL in Escherichia coli and investigated the oligomeric state of TetL in the membrane and in detergent solution. Evidence for an oligomeric state of TetL emerged from SDS-PAGE and Western blot analysis of membrane samples as well as purified protein samples from cells that expressed two differently tagged TetL species. Furthermore, no formation or restoration of TetL oligomers occurred upon detergent solubilization of the membrane. Rather, oligomeric forms established in vivo persisted after solubilization. Mass spectrometry of the purified protein showed the absence of proteolysis and posttranslational modifications. Analytical size-exclusion chromatography of the purified protein revealed a dimeric TetL in dodecyl-maltoside solution. In addition, TetL dimers were found in a number of other detergents and over a wide pH range. It is therefore likely that the oligomeric form of the protein in the membrane is also a dimer.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.