Going Outside the TonB Box: Identification of Novel FepA-TonB Interactions In Vivo
نویسندگان
چکیده
منابع مشابه
Regions of Escherichia coli TonB and FepA proteins essential for in vivo physical interactions.
The transport of Fe(III)-siderophore complexes and vitamin B12 across the outer membrane of Escherichia coli is an active transport process requiring a cognate outer membrane receptor, cytoplasmic membrane-derived proton motive force, and an energy-transducing protein anchored in the cytoplasmic membrane, TonB. This process requires direct physical contact between the outer membrane receptor an...
متن کاملIn vivo inhibition of TonB-dependent processes by a TonB box consensus pentapeptide.
The TonB box, a conserved pentapeptide sequence found in TonB-dependent colicins and receptors, is thought to interact physically with the TonB protein to facilitate TonB-dependent processes. Strains of Escherichia coli were treated in vivo with the synthetic TonB box pentapeptide Glu-Thr-Val-Ile-Val. The pentapeptide inhibited several TonB-dependent processes, including cell growth in low-iron...
متن کاملConfined Mobility of TonB and FepA in Escherichia coli Membranes
The important process of nutrient uptake in Escherichia coli, in many cases, involves transit of the nutrient through a class of beta-barrel proteins in the outer membrane known as TonB-dependent transporters (TBDTs) and requires interaction with the inner membrane protein TonB. Here we have imaged the mobility of the ferric enterobactin transporter FepA and TonB by tracking them in the membran...
متن کاملInteractions between the outer membrane ferric citrate transporter FecA and TonB: studies of the FecA TonB box.
Both induction of transcription of the ferric citrate transport genes and transport of ferric citrate by the Escherichia coli outer membrane receptor FecA require energy derived from the proton motive force (PMF) of the inner membrane. The energy is transduced to FecA by the inner membrane complex, TonB, ExbB, and ExbD. Region 160 of TonB and the conserved TonB box of other TonB-dependent recep...
متن کاملIdentification of functionally important TonB-ExbD periplasmic domain interactions in vivo.
In gram-negative bacteria, the cytoplasmic membrane proton-motive force energizes the active transport of TonB-dependent ligands through outer membrane TonB-gated transporters. In Escherichia coli, cytoplasmic membrane proteins ExbB and ExbD couple the proton-motive force to conformational changes in TonB, which are hypothesized to form the basis of energy transduction through direct contact wi...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 2017
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.00649-16