ATP-driven Na+ transport and Na(+)-dependent ATP synthesis in Escherichia coli grown at low delta mu H
In inverted subcellular vesicles of Escherichia coli grown at high delta mu H+ (neutral pH, no protonophorous uncoupler), ATP-driven Na+ transport and oxidative phosphorylation are completely inhibited by the protonophore CCCP. If E. coli was grown at low delta mu H+, i.e. at high pH or in the prese...
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Veröffentlicht in: | FEBS letters 1993-02, Vol.317 (3), p.267-270 |
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creator | Avetisyan, A V Bogachev, A V Murtasina, R A Skulachev, V P |
description | In inverted subcellular vesicles of Escherichia coli grown at high delta mu H+ (neutral pH, no protonophorous uncoupler), ATP-driven Na+ transport and oxidative phosphorylation are completely inhibited by the protonophore CCCP. If E. coli was grown at low delta mu H+, i.e. at high pH or in the presence of uncoupler, some oxidative phosphorylation was observed in the vesicles even in CCCP-containing medium, and Na+ transport was actually stimulated by CCCP. The CCCP-resistant transport and phosphorylation were absent from the unc mutant lacking F0F1 ATPase. Both processes proved to be sensitive to (i) the Na+/H+ antiporter monensin, (ii) the Na+ uniporter ETH 157, (iii) the F0 inhibitors DCCD and venturicidin, and (iv) the F1 inhibitor aurovertin. The CCCP-resistant oxidative phosphorylation was stimulated by Na+ and arrested by oppositely directed delta pNa. These data are consistent with the assumption that, under appropriate growth conditions, the F0F1-type ATPase of E. coli becomes competent in transporting Na+ ions. |
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If E. coli was grown at low delta mu H+, i.e. at high pH or in the presence of uncoupler, some oxidative phosphorylation was observed in the vesicles even in CCCP-containing medium, and Na+ transport was actually stimulated by CCCP. The CCCP-resistant transport and phosphorylation were absent from the unc mutant lacking F0F1 ATPase. Both processes proved to be sensitive to (i) the Na+/H+ antiporter monensin, (ii) the Na+ uniporter ETH 157, (iii) the F0 inhibitors DCCD and venturicidin, and (iv) the F1 inhibitor aurovertin. The CCCP-resistant oxidative phosphorylation was stimulated by Na+ and arrested by oppositely directed delta pNa. 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If E. coli was grown at low delta mu H+, i.e. at high pH or in the presence of uncoupler, some oxidative phosphorylation was observed in the vesicles even in CCCP-containing medium, and Na+ transport was actually stimulated by CCCP. The CCCP-resistant transport and phosphorylation were absent from the unc mutant lacking F0F1 ATPase. Both processes proved to be sensitive to (i) the Na+/H+ antiporter monensin, (ii) the Na+ uniporter ETH 157, (iii) the F0 inhibitors DCCD and venturicidin, and (iv) the F1 inhibitor aurovertin. The CCCP-resistant oxidative phosphorylation was stimulated by Na+ and arrested by oppositely directed delta pNa. These data are consistent with the assumption that, under appropriate growth conditions, the F0F1-type ATPase of E. coli becomes competent in transporting Na+ ions.</description><subject>Adenosine Triphosphatases - antagonists & inhibitors</subject><subject>Adenosine Triphosphatases - metabolism</subject><subject>Adenosine Triphosphate - biosynthesis</subject><subject>Adenosine Triphosphate - physiology</subject><subject>Biological Transport, Active - physiology</subject><subject>Dicyclohexylcarbodiimide - pharmacology</subject><subject>Electron Transport - physiology</subject><subject>Escherichia coli - drug effects</subject><subject>Escherichia coli - metabolism</subject><subject>Hydrogen-Ion Concentration</subject><subject>Oxidative Phosphorylation - drug effects</subject><subject>Sodium - metabolism</subject><subject>Sodium - physiology</subject><subject>Uncoupling Agents - pharmacology</subject><issn>0014-5793</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNotkE1Lw0AYhPeg1Fr9CcJ7EqUEmmz2I8dSaisUFew9bHbf2JVkE3c3lv57A-Y0zPAwDHNF5qtVmidMFPSG3IbwvRq9TIsZmck8Yzzlc1Kvjx-J8fYXHbypJUSvXOg7H0E5MyZPy-fEYI_OoIswwhAuLp4w2ADWwTboE3qrT1aB7hoLX747O1ARmu4MBpuooB1gf0eua9UEvJ90QT5ftsfNPjm8714360PSM8oTWalqXCgwrTkrikrwIme65poJVhueVdTIMUORy0whzSRNJRUs11JrKjRdkMf_1t53PwOGWLY2aGwa5bAbQikYy6UU6Qg-TOBQtWjK3ttW-Us53UL_AEbnW7k</recordid><startdate>19930215</startdate><enddate>19930215</enddate><creator>Avetisyan, A V</creator><creator>Bogachev, A V</creator><creator>Murtasina, R A</creator><creator>Skulachev, V P</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>19930215</creationdate><title>ATP-driven Na+ transport and Na(+)-dependent ATP synthesis in Escherichia coli grown at low delta mu H</title><author>Avetisyan, A V ; Bogachev, A V ; Murtasina, R A ; Skulachev, V P</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p536-8bab0187e1f6599b76945cf6c575fd62b3d8769e7482ae3283183754c8cc37c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Adenosine Triphosphatases - antagonists & inhibitors</topic><topic>Adenosine Triphosphatases - metabolism</topic><topic>Adenosine Triphosphate - biosynthesis</topic><topic>Adenosine Triphosphate - physiology</topic><topic>Biological Transport, Active - physiology</topic><topic>Dicyclohexylcarbodiimide - pharmacology</topic><topic>Electron Transport - physiology</topic><topic>Escherichia coli - drug effects</topic><topic>Escherichia coli - metabolism</topic><topic>Hydrogen-Ion Concentration</topic><topic>Oxidative Phosphorylation - drug effects</topic><topic>Sodium - metabolism</topic><topic>Sodium - physiology</topic><topic>Uncoupling Agents - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Avetisyan, A V</creatorcontrib><creatorcontrib>Bogachev, A V</creatorcontrib><creatorcontrib>Murtasina, R A</creatorcontrib><creatorcontrib>Skulachev, V P</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Avetisyan, A V</au><au>Bogachev, A V</au><au>Murtasina, R A</au><au>Skulachev, V P</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>ATP-driven Na+ transport and Na(+)-dependent ATP synthesis in Escherichia coli grown at low delta mu H</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1993-02-15</date><risdate>1993</risdate><volume>317</volume><issue>3</issue><spage>267</spage><epage>270</epage><pages>267-270</pages><issn>0014-5793</issn><abstract>In inverted subcellular vesicles of Escherichia coli grown at high delta mu H+ (neutral pH, no protonophorous uncoupler), ATP-driven Na+ transport and oxidative phosphorylation are completely inhibited by the protonophore CCCP. If E. coli was grown at low delta mu H+, i.e. at high pH or in the presence of uncoupler, some oxidative phosphorylation was observed in the vesicles even in CCCP-containing medium, and Na+ transport was actually stimulated by CCCP. The CCCP-resistant transport and phosphorylation were absent from the unc mutant lacking F0F1 ATPase. Both processes proved to be sensitive to (i) the Na+/H+ antiporter monensin, (ii) the Na+ uniporter ETH 157, (iii) the F0 inhibitors DCCD and venturicidin, and (iv) the F1 inhibitor aurovertin. The CCCP-resistant oxidative phosphorylation was stimulated by Na+ and arrested by oppositely directed delta pNa. These data are consistent with the assumption that, under appropriate growth conditions, the F0F1-type ATPase of E. coli becomes competent in transporting Na+ ions.</abstract><cop>England</cop><pmid>8425616</pmid><tpages>4</tpages></addata></record> |
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subjects | Adenosine Triphosphatases - antagonists & inhibitors Adenosine Triphosphatases - metabolism Adenosine Triphosphate - biosynthesis Adenosine Triphosphate - physiology Biological Transport, Active - physiology Dicyclohexylcarbodiimide - pharmacology Electron Transport - physiology Escherichia coli - drug effects Escherichia coli - metabolism Hydrogen-Ion Concentration Oxidative Phosphorylation - drug effects Sodium - metabolism Sodium - physiology Uncoupling Agents - pharmacology |
title | ATP-driven Na+ transport and Na(+)-dependent ATP synthesis in Escherichia coli grown at low delta mu H |
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