Requirements for Osmosensing and Osmotic Activation of Transporter ProP from Escherichia coli

Transporter ProP of Escherichia coli, a solute-H+ symporter, can sense and respond to osmotic upshifts imposed on cells, on membrane vesicles, or on proteoliposomes that incorporate purified ProP-(His)6. In this study, proline uptake catalyzed by ProP was used as a measure of its osmotic activation,...

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Veröffentlicht in:Biochemistry (Easton) 2001-06, Vol.40 (24), p.7324-7333
Hauptverfasser: Racher, Kathleen I, Culham, Doreen E, Wood, Janet M
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container_title Biochemistry (Easton)
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creator Racher, Kathleen I
Culham, Doreen E
Wood, Janet M
description Transporter ProP of Escherichia coli, a solute-H+ symporter, can sense and respond to osmotic upshifts imposed on cells, on membrane vesicles, or on proteoliposomes that incorporate purified ProP-(His)6. In this study, proline uptake catalyzed by ProP was used as a measure of its osmotic activation, and the requirements for osmosensing were defined using the proteoliposome system. The initial rate of proline uptake increased with decreasing external pH and increasing ΔΨ, lumen negative. Osmotic upshifts increased ΔΨ by concentrating lumenal K+, but osmotic activation of ProP could be distinguished from this effect. Osmotic activation of ProP resulted from changes in V max, though osmotic shifts also increased the K M for proline. Osmotic activation could be described as a reversible, osmotic upshift-dependent transition linking (at least) two transporter protein conformations. No correlation was observed between ProP activation and the position of the anions of activating sodium salts within the Hofmeister series of solutes. Both the magnitude of the osmotic upshift required to activate ProP and the ProP activity attained were similar for membrane-impermeant osmolytes, including NaCl, glucose, and PEG 600. The membrane-permeant osmolytes glycerol, urea, PEG 62, and PEG 106 failed to activate ProP. Two poly(ethylene glycol)s, PEG 150 and PEG 200, were membrane-permeant and did not cause liposome shrinkage, but they did partially activate ProP-(His)6.
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subjects Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Bacterial Proteins - physiology
Carrier Proteins - genetics
Carrier Proteins - metabolism
Carrier Proteins - physiology
Escherichia coli
Escherichia coli - genetics
Escherichia coli - metabolism
Escherichia coli - physiology
Escherichia coli Proteins
Glucosides - pharmacology
Histidine - genetics
Hydrogen-Ion Concentration
Kinetics
Liposomes - metabolism
Membrane Potentials - drug effects
Membrane Potentials - genetics
Osmolar Concentration
Osmotic Pressure - drug effects
Plasmids - metabolism
Polyethylene Glycols - pharmacology
ProP protein
Proteolipids - genetics
Proteolipids - metabolism
Proteolipids - physiology
Sodium Chloride - pharmacology
Solutions
Symporters
transporters
title Requirements for Osmosensing and Osmotic Activation of Transporter ProP from Escherichia coli
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