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!align=left |Citation | |||
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'''Sato, M, Machida, K, Arikado, E, Saito, H, Kakegawa, T and Kobayashi, H''' (2000) Expression of outer membrane proteins in Escherichia coli growing at acid pH. ''Appl. Environ. Microbiol.'' '''66''':943-7 | |||
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!align=left |Abstract | |||
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It is generally accepted for Escherichia coli that (i) the level of OmpC increases with increased osmolarity when cells are growing in neutral and alkaline media, whereas the level of OmpF decreases at high osmolarity, and that (ii) the two-component system composed of OmpR (regulator) and EnvZ (sensor) regulates porin expression. In this study, we found that OmpC was expressed at low osmolarity in medium of pH below 6 and that the expression was repressed when medium osmolarity was increased. In contrast, the expression of ompF at acidic pH was essentially the same as that at alkaline pH. Neither OmpC nor OmpF was detectable in an ompR mutant at both acid and alkaline pH values. However, OmpC and OmpF were well expressed at acid pH in a mutant envZ strain, and their expression was regulated by medium osmolarity. Thus, it appears that E. coli has a different mechanism for porin expression at acid pH. A mutant deficient in ompR grew slower than its parent strain in low-osmolarity medium at acid pH (below 5.5). The same growth diminution was observed when ompC and ompF were deleted, suggesting that both OmpF and OmpC are required for optimal growth under hypoosmosis at acid pH. | |||
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=10698756 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC91927 PMC91927] | |||
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| | !align=left |Keywords | ||
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|- | Acids; Bacterial Outer Membrane Proteins/biosynthesis; Bacterial Proteins; Escherichia coli/metabolism; Escherichia coli Proteins; Hydrogen-Ion Concentration; Multienzyme Complexes; Osmolar Concentration; Porins/biosynthesis; Trans-Activators/genetics | ||
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==Significance {{HelpIcon|Help:Literature}} == | ==Significance {{HelpIcon|Help:Literature}} == | ||
{{LitSignificance}} | {{LitSignificance}} | ||
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==Annotations {{HelpIcon|Help:Literature}}== | ==Annotations {{HelpIcon|Help:Literature}}== | ||
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==EcoliWiki Links {{HelpIcon|Help:Literature}} == | ==EcoliWiki Links {{HelpIcon|Help:Literature}} == | ||
Latest revision as of 04:11, 15 September 2013
| Citation |
Sato, M, Machida, K, Arikado, E, Saito, H, Kakegawa, T and Kobayashi, H (2000) Expression of outer membrane proteins in Escherichia coli growing at acid pH. Appl. Environ. Microbiol. 66:943-7 |
|---|---|
| Abstract |
It is generally accepted for Escherichia coli that (i) the level of OmpC increases with increased osmolarity when cells are growing in neutral and alkaline media, whereas the level of OmpF decreases at high osmolarity, and that (ii) the two-component system composed of OmpR (regulator) and EnvZ (sensor) regulates porin expression. In this study, we found that OmpC was expressed at low osmolarity in medium of pH below 6 and that the expression was repressed when medium osmolarity was increased. In contrast, the expression of ompF at acidic pH was essentially the same as that at alkaline pH. Neither OmpC nor OmpF was detectable in an ompR mutant at both acid and alkaline pH values. However, OmpC and OmpF were well expressed at acid pH in a mutant envZ strain, and their expression was regulated by medium osmolarity. Thus, it appears that E. coli has a different mechanism for porin expression at acid pH. A mutant deficient in ompR grew slower than its parent strain in low-osmolarity medium at acid pH (below 5.5). The same growth diminution was observed when ompC and ompF were deleted, suggesting that both OmpF and OmpC are required for optimal growth under hypoosmosis at acid pH. |
| Links | |
| Keywords |
Acids; Bacterial Outer Membrane Proteins/biosynthesis; Bacterial Proteins; Escherichia coli/metabolism; Escherichia coli Proteins; Hydrogen-Ion Concentration; Multienzyme Complexes; Osmolar Concentration; Porins/biosynthesis; Trans-Activators/genetics |
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