Visualization of AqpZ-mediated water permeability in Escherichia coli by cryoelectron microscopy.
Transport of water across the plasma membrane is a fundamental process occurring in all living organisms. In bacteria, osmotic movement of water across the cytoplasmic membrane is needed to maintain cellular turgor; however, the molecular mechanisms of this process are poorly defined. Involvement of aquaporin water channels in bacterial water permeability was suggested by the recent discovery of the aquaporin gene, aqpZ, in Escherichia coli. By employing cryoelectron microscopy to compare E. coli cells containing (AqpZ+) and lacking (AqpZ-) aquaporin, we show that the AqpZ water channel rapidly mediates large water fluxes in response to sudden changes in extracellular osmolarity. These findings (i) demonstrate for the first time functional expression of a prokaryotic water channel, (ii) evidence the bidirectional water channel feature of AqpZ, (iii) document a role for AqpZ in bacterial osmoregulation, and (iv) define a suitable model for studying the physiology of prokaryotic water transport.
UPRES-A CNRS 6026, Biologie Cellulaire et Reproduction, Equipe Canaux et Récepteurs Membranaires, Université de Rennes 1, Campus de Beaulieu, 35042 Rennes Cedex, France.
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Delamarche
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Thomas
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JP
Rolland
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Froger
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Gouranton
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Svelto
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Agre
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Calamita
D020346:Aquaporins / Q000235:genetics / Q000502:physiology*; D002463:Cell Membrane Permeability / Q000187:drug effects* / Q000502:physiology*; D020285:Cryoelectron Microscopy / Q000379:methods*; D004926:Escherichia coli / Q000235:genetics / Q000502:physiology*; D029968:Escherichia coli Proteins; D008565:Membrane Proteins; D009994:Osmolar Concentration; D014867:Water / Q000378:metabolism*
D020346:Aquaporins; D029968:Escherichia coli Proteins; D008565:Membrane Proteins; C106425:aqpZ protein, E coli; D014867:Water