PMID:10400575: Difference between revisions

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<span style = 'font-size: large'> '''Delamarche, C, Thomas, D, Rolland, JP, Froger, A, Gouranton, J, Svelto, M, Agre, P and Calamita, G'''  (1999) Visualization of AqpZ-mediated water permeability in Escherichia coli by cryoelectron microscopy.''J. Bacteriol.'' '''181''':4193-7</span>
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!align=left  |Citation
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'''Delamarche, C, Thomas, D, Rolland, JP, Froger, A, Gouranton, J, Svelto, M, Agre, P and Calamita, G'''  (1999) Visualization of AqpZ-mediated water permeability in Escherichia coli by cryoelectron microscopy. ''J. Bacteriol.'' '''181''':4193-7
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!align=left  |Abstract
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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.
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!align=left  |Links
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=10400575 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC93919 PMC93919]


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|{{TableHeadingColor}} |'''Abstract''' || 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.
!align=left  |Keywords
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Aquaporins/genetics; Aquaporins/physiology; Cell Membrane Permeability/drug effects; Cell Membrane Permeability/physiology; Cryoelectron Microscopy/methods; Escherichia coli/genetics; Escherichia coli/physiology; Escherichia coli Proteins; Membrane Proteins; Osmolar Concentration; Water/metabolism
|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=10400575 PubMed]
 
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Latest revision as of 04:10, 15 September 2013

Citation

Delamarche, C, Thomas, D, Rolland, JP, Froger, A, Gouranton, J, Svelto, M, Agre, P and Calamita, G (1999) Visualization of AqpZ-mediated water permeability in Escherichia coli by cryoelectron microscopy. J. Bacteriol. 181:4193-7

Abstract

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.

Links

PubMed PMC93919

Keywords

Aquaporins/genetics; Aquaporins/physiology; Cell Membrane Permeability/drug effects; Cell Membrane Permeability/physiology; Cryoelectron Microscopy/methods; Escherichia coli/genetics; Escherichia coli/physiology; Escherichia coli Proteins; Membrane Proteins; Osmolar Concentration; Water/metabolism

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