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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
7
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pubmed:dateCreated |
1994-3-16
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pubmed:abstractText |
Glucose limitation in chemostats derepressed the binding-protein-dependent Mgl transport system, which is strongly repressed during growth in batch culture with high glucose levels. The limitation-induced Mgl activity was higher than that of batch cultures "fully induced" for the Mgl system after growth on glycerol plus fucose. Mgl- strains were impaired compared to Mgl+ bacteria in removing glucose from sugar-limited chemostats and were outcompeted in mixed continuous culture on limiting glucose. The influence of Mgl was not observed on growth with limiting maltose or non-carbohydrates, and thus was specific for glucose, a known substrate of the Mgl system. In the absence of the two glucose-specific membrane components of the phosphoenolpyruvate:sugar phosphotransferase system, non-PTS-dependent growth on glucose was observed in continuous culture, but only under sugar-limited conditions derepressing the Mgl system and not in glucose-rich batches or continuous culture. Hence growth of Escherichia coli on glucose at micromolar concentrations involves a significant contribution of a binding-protein-dependent transport system. The participation of multiple transporters in glucose transport can account for the complex non-hyperbolic dependence of growth-rate on glucose concentration and for discrepancies in studies attempting to describe growth on glucose purely in terms of phosphotransferase kinetics.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Culture Media,
http://linkedlifedata.com/resource/pubmed/chemical/Galactose,
http://linkedlifedata.com/resource/pubmed/chemical/Glucose,
http://linkedlifedata.com/resource/pubmed/chemical/Maltose,
http://linkedlifedata.com/resource/pubmed/chemical/Methylgalactosides,
http://linkedlifedata.com/resource/pubmed/chemical/Monosaccharide Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoenolpyruvate Sugar...
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0923-2508
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
144
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
529-37
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8310178-Biological Transport, Active,
pubmed-meshheading:8310178-Culture Media,
pubmed-meshheading:8310178-Escherichia coli,
pubmed-meshheading:8310178-Galactose,
pubmed-meshheading:8310178-Glucose,
pubmed-meshheading:8310178-Maltose,
pubmed-meshheading:8310178-Methylgalactosides,
pubmed-meshheading:8310178-Monosaccharide Transport Proteins,
pubmed-meshheading:8310178-Phosphoenolpyruvate Sugar Phosphotransferase System
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pubmed:year |
1993
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pubmed:articleTitle |
The importance of the binding-protein-dependent Mgl system to the transport of glucose in Escherichia coli growing on low sugar concentrations.
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pubmed:affiliation |
Department of Microbiology, University of Sydney, N.S.W., Australia.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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