Expression of outer membrane proteins in Escherichia coli growing at acid pH
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 (sen...
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description | 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. |
doi_str_mv | 10.1128/AEM.66.3.943-947.2000 |
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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.</description><identifier>ISSN: 0099-2240</identifier><identifier>EISSN: 1098-5336</identifier><identifier>DOI: 10.1128/AEM.66.3.943-947.2000</identifier><identifier>PMID: 10698756</identifier><identifier>CODEN: AEMIDF</identifier><language>eng</language><publisher>Washington, DC: American Society for Microbiology</publisher><subject>Acids ; Bacteria ; Bacterial Outer Membrane Proteins - biosynthesis ; Bacterial Proteins ; Bacteriology ; Biological and medical sciences ; EnvZ protein ; Escherichia coli ; Escherichia coli - metabolism ; Escherichia coli Proteins ; Fundamental and applied biological sciences. Psychology ; Genetics ; Hydrogen-Ion Concentration ; Membranes ; Microbiology ; Multienzyme Complexes ; OmpC protein ; OmpF protein ; Osmolar Concentration ; Physiology and Biotechnology ; Porins - biosynthesis ; Proteins ; Trans-Activators - genetics</subject><ispartof>Applied and environmental microbiology, 2000-03, Vol.66 (3), p.943-947</ispartof><rights>2000 INIST-CNRS</rights><rights>Copyright American Society for Microbiology Mar 2000</rights><rights>Copyright © 2000, American Society for Microbiology 2000</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c544t-9752ffafa528bffbb5c0cfe3b95154af40b60290ce390d5797b45d9c5c8cf3d03</citedby><cites>FETCH-LOGICAL-c544t-9752ffafa528bffbb5c0cfe3b95154af40b60290ce390d5797b45d9c5c8cf3d03</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC91927/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC91927/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,3174,27903,27904,53770,53772</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=1296868$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10698756$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>SATO, M</creatorcontrib><creatorcontrib>MACHIDA, K</creatorcontrib><creatorcontrib>ARIKADO, E</creatorcontrib><creatorcontrib>SAITO, H</creatorcontrib><creatorcontrib>KAKEGAWA, T</creatorcontrib><creatorcontrib>KOBAYASHI, H</creatorcontrib><title>Expression of outer membrane proteins in Escherichia coli growing at acid pH</title><title>Applied and environmental microbiology</title><addtitle>Appl Environ Microbiol</addtitle><description>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.</description><subject>Acids</subject><subject>Bacteria</subject><subject>Bacterial Outer Membrane Proteins - biosynthesis</subject><subject>Bacterial Proteins</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>EnvZ protein</subject><subject>Escherichia coli</subject><subject>Escherichia coli - metabolism</subject><subject>Escherichia coli Proteins</subject><subject>Fundamental and applied biological sciences. 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Psychology</topic><topic>Genetics</topic><topic>Hydrogen-Ion Concentration</topic><topic>Membranes</topic><topic>Microbiology</topic><topic>Multienzyme Complexes</topic><topic>OmpC protein</topic><topic>OmpF protein</topic><topic>Osmolar Concentration</topic><topic>Physiology and Biotechnology</topic><topic>Porins - biosynthesis</topic><topic>Proteins</topic><topic>Trans-Activators - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>SATO, M</creatorcontrib><creatorcontrib>MACHIDA, K</creatorcontrib><creatorcontrib>ARIKADO, E</creatorcontrib><creatorcontrib>SAITO, H</creatorcontrib><creatorcontrib>KAKEGAWA, T</creatorcontrib><creatorcontrib>KOBAYASHI, H</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Environment Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>Environment Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Applied and environmental microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>SATO, M</au><au>MACHIDA, K</au><au>ARIKADO, E</au><au>SAITO, H</au><au>KAKEGAWA, T</au><au>KOBAYASHI, H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Expression of outer membrane proteins in Escherichia coli growing at acid pH</atitle><jtitle>Applied and environmental microbiology</jtitle><addtitle>Appl Environ Microbiol</addtitle><date>2000-03-01</date><risdate>2000</risdate><volume>66</volume><issue>3</issue><spage>943</spage><epage>947</epage><pages>943-947</pages><issn>0099-2240</issn><eissn>1098-5336</eissn><coden>AEMIDF</coden><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.</abstract><cop>Washington, DC</cop><pub>American Society for Microbiology</pub><pmid>10698756</pmid><doi>10.1128/AEM.66.3.943-947.2000</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Acids Bacteria Bacterial Outer Membrane Proteins - biosynthesis Bacterial Proteins Bacteriology Biological and medical sciences EnvZ protein Escherichia coli Escherichia coli - metabolism Escherichia coli Proteins Fundamental and applied biological sciences. Psychology Genetics Hydrogen-Ion Concentration Membranes Microbiology Multienzyme Complexes OmpC protein OmpF protein Osmolar Concentration Physiology and Biotechnology Porins - biosynthesis Proteins Trans-Activators - genetics |
title | Expression of outer membrane proteins in Escherichia coli growing at acid pH |
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