Regions of Escherichia coli TonB and FepA proteins essential for in vivo physical interactions
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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 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 کاملCharacterization of in vitro interactions between a truncated TonB protein from Escherichia coli and the outer membrane receptors FhuA and FepA.
High-affinity iron uptake in gram-negative bacteria depends upon TonB, a protein which couples the proton motive force in the cytoplasmic membrane to iron chelate receptors in the outer membrane. To advance studies on TonB structure and function, we expressed a recombinant form of Escherichia coli TonB lacking the N-terminal cytoplasmic membrane anchor. This protein (H(6)-'TonB; M(r), 24,880) w...
متن کاملStaphylococcus aureus FepA and FepB Proteins Drive Heme Iron Utilization in Escherichia coli
EfeUOB-like tripartite systems are widespread in bacteria and in many cases they are encoded by genes organized into iron-regulated operons. They consist of: EfeU, a protein similar to the yeast iron permease Ftrp1; EfeO, an extracytoplasmic protein of unknown function and EfeB, also an extracytoplasmic protein with heme peroxidase activity, belonging to the DyP family. Many bacterial EfeUOB sy...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1997
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.179.10.3213-3221.1997