ArticleThe Journal of biological chemistry2016
Disulfide Cross-linking of a Multidrug and Toxic Compound Extrusion Transporter Impacts Multidrug Efflux.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 16 citations in OpenAlex.
- Genome-wide mining and characterization of MATE transporters in Coriandrum sativum L.Molecular biology research communications · 2024Article
- Genome wide identification and characterization of MATE family genes in mangrove plants.Genetica · 2023Article
- Antimicrobial Resistance and Inorganic Nanoparticles.International journal of molecular sciences · 2021Review
- Principles of Alternating Access in Multidrug and Toxin Extrusion (MATE) Transporters.Journal of molecular biology · 2021Review
- Genome-wide characterization of MATE gene family and expression profiles in response to abiotic stresses in rice (Oryza sativa).BMC ecology and evolution · 2021Article
- The N-terminal domain of an archaeal multidrug and toxin extrusion (MATE) transporter mediates proton coupling required for prokaryotic drug resistance.The Journal of biological chemistry · 2019Article
- Probing Conformational States of a Target Protein inBio-protocol · 2019Article
- Multidrug efflux pumps: structure, function and regulation.Nature reviews. Microbiology · 2018Review
- Sodium and proton coupling in the conformational cycle of a MATE antiporter fromProceedings of the National Academy of Sciences of the United States of America · 2018Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Multidrug and toxic compound extrusion (MATE) transporters contribute to multidrug resistance by extruding different drugs across cell membranes. The MATE transporters alternate between their extracellular and intracellular facing conformations to propel drug export, but how these structural changes occur is unclear. Here we combine site-specific cross-linking and functional studies to probe the movement of transmembrane helices in NorM from Neiserria gonorrheae (NorM-NG), a MATE transporter with known extracellular facing structure. We generated an active, cysteine-less NorM-NG and conducted pairwise cysteine mutagenesis on this variant. We found that copper phenanthroline catalyzed disulfide bond formation within five cysteine pairs and increased the electrophoretic mobility of the corresponding mutants. Furthermore, copper phenanthroline abolished the activity of the five paired cysteine mutants, suggesting that these substituted amino acids come in spatial proximity during transport, and the proximity changes are functionally indispensable. Our data also implied that the substrate-binding transmembrane helices move up to 10 Å in NorM-NG during transport and afforded distance restraints for modeling the intracellular facing transporter, thereby casting new light on the underlying mechanism.
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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.