Gating of TonB-dependent transporters by substrate-specific forced remodelling
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چکیده
منابع مشابه
Gating of TonB-dependent transporters by substrate-specific forced remodelling
Membrane proteins play vital roles in inside-out and outside-in signal transduction by responding to inputs that include mechanical stimuli. Mechanical gating may be mediated by the membrane or by protein(s) but evidence for the latter is scarce. Here we use force spectroscopy, protein engineering and bacterial growth assays to investigate the effects of force on complexes formed between TonB a...
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Transcription of the ferric citrate import system is regulated by ferric citrate binding to the outer membrane transporter FecA. A signal indicating transporter occupancy is relayed across the outer membrane to energy-transducing and regulatory proteins embedded in the cytoplasmic membrane. Because transcriptional activation is not coupled to ferric citrate import, an allosteric mechanism under...
متن کاملSubstrate-dependent transmembrane signaling in TonB-dependent transporters is not conserved.
Site-directed spin labeling (SDSL) was used to examine and compare transmembrane signaling events in the bacterial outer-membrane transport proteins BtuB, FecA, and FhuA. These proteins extract energy for transport by coupling to the transperiplasmic protein TonB, an interaction that is thought to be mediated by the Ton box, a highly conserved energy-coupling motif in these transporters. In the...
متن کاملDifferential substrate-induced signaling through the TonB-dependent transporter BtuB.
The BtuB transporter mediates high-affinity binding and TonB-dependent active transport of vitamin B12 [cyanocobalamin (CNCbl)] across the outer membrane of Escherichia coli. A characteristic feature of TonB-dependent transporters is the Ton box, a conserved sequence near the N terminus and exposed to the periplasm. Crosslinking to TonB and site-directed spin labeling indicated that the Ton box...
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ژورنال
عنوان ژورنال: Nature Communications
سال: 2017
ISSN: 2041-1723
DOI: 10.1038/ncomms14804