LotaV3, Istex, Corpus, bibRecord, 001687

Mutations in the MotA protein of Escherichia coli reveal domains critical for proton conduction

Identifieur interne : 001687 ( Istex/Corpus ); précédent : 001686; suivant : 001688

Mutations in the MotA protein of Escherichia coli reveal domains critical for proton conduction

Auteurs : David F. Blair ; Howard C. Berg

Source :

Journal of Molecular Biology [ 0022-2836 ] ; 1991.

RBID : ISTEX:83D3D4E11CA2F46B951F5AEF8178FB808CF57DAA

English descriptors

KwdEn :
- PMSF, bR, bacterial motility, flagellar rotation, ion channels, membrane proteins, random mutagenesis.

Abstract

The MotA protein of Escherichia coli is an essential component of the torque-generating units that drive the flagellar rotary motor. A variety of evidence indicates that MotA is involved in transmembrane proton conduction. We have now mapped a number of MotA mutants, focusing primarily on those previously shown to be dominant. Fifty-six mutations (all dominant), each causing severe or complete impairment of function, were sequenced and found to correspond to 31 different alleles. All except two of these encoded amino acid substitutions clustered in four hydrophobic, presumably membrane-spanning segments, that together make up only one-third of the length of the polypeptide chain. In contrast, eight mutations (5 dominant), each causing only slight impairment of function (slow alleles), were sequenced and found to specify amino acid substitutions in three hydrophilic domains. The clustering of the mutations provides independent support for the suggestion that MotA is a transmembrane proton channel and places significant constraints on models for the molecular mechanism of ion conduction.

Url:

https://api.istex.fr/document/83D3D4E11CA2F46B951F5AEF8178FB808CF57DAA/fulltext/pdf

DOI: 10.1016/0022-2836(91)90943-Z

Links to Exploration step

ISTEX:83D3D4E11CA2F46B951F5AEF8178FB808CF57DAA

Le document en format XML

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<front><div type="abstract" xml:lang="en">The MotA protein of Escherichia coli is an essential component of the torque-generating units that drive the flagellar rotary motor. A variety of evidence indicates that MotA is involved in transmembrane proton conduction. We have now mapped a number of MotA mutants, focusing primarily on those previously shown to be dominant. Fifty-six mutations (all dominant), each causing severe or complete impairment of function, were sequenced and found to correspond to 31 different alleles. All except two of these encoded amino acid substitutions clustered in four hydrophobic, presumably membrane-spanning segments, that together make up only one-third of the length of the polypeptide chain. In contrast, eight mutations (5 dominant), each causing only slight impairment of function (slow alleles), were sequenced and found to specify amino acid substitutions in three hydrophilic domains. The clustering of the mutations provides independent support for the suggestion that MotA is a transmembrane proton channel and places significant constraints on models for the molecular mechanism of ion conduction.</div>
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<abstract xml:lang="en"><p>The MotA protein of Escherichia coli is an essential component of the torque-generating units that drive the flagellar rotary motor. A variety of evidence indicates that MotA is involved in transmembrane proton conduction. We have now mapped a number of MotA mutants, focusing primarily on those previously shown to be dominant. Fifty-six mutations (all dominant), each causing severe or complete impairment of function, were sequenced and found to correspond to 31 different alleles. All except two of these encoded amino acid substitutions clustered in four hydrophobic, presumably membrane-spanning segments, that together make up only one-third of the length of the polypeptide chain. In contrast, eight mutations (5 dominant), each causing only slight impairment of function (slow alleles), were sequenced and found to specify amino acid substitutions in three hydrophilic domains. The clustering of the mutations provides independent support for the suggestion that MotA is a transmembrane proton channel and places significant constraints on models for the molecular mechanism of ion conduction.</p>
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<head><ce:article-footnote><ce:note-para>This work was supported by NSF grant DCB-8903690.</ce:note-para>
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<ce:title>Mutations in the MotA protein of <ce:italic>Escherichia coli</ce:italic>
 reveal domains critical for proton conduction</ce:title>
<ce:author-group><ce:author><ce:given-name>David F.</ce:given-name>
<ce:surname>Blair</ce:surname>
<ce:cross-ref refid="fn1"><ce:sup>†</ce:sup>
</ce:cross-ref>
</ce:author>
<ce:author><ce:given-name>Howard C.</ce:given-name>
<ce:surname>Berg</ce:surname>
</ce:author>
<ce:affiliation><ce:textfn>Department of Cellular and Developmental Biology, Harvard University 16 Divinity Avenue, Cambridge, MA 02138 USA</ce:textfn>
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<ce:footnote id="fn1"><ce:label>†</ce:label>
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<ce:abstract id="ab1" class="author" xml:lang="en"><ce:section-title>Abstract</ce:section-title>
<ce:abstract-sec><ce:simple-para>The MotA protein of <ce:italic>Escherichia coli</ce:italic>
 is an essential component of the torque-generating units that drive the flagellar rotary motor. A variety of evidence indicates that MotA is involved in transmembrane proton conduction. We have now mapped a number of MotA mutants, focusing primarily on those previously shown to be dominant. Fifty-six mutations (all dominant), each causing severe or complete impairment of function, were sequenced and found to correspond to 31 different alleles. All except two of these encoded amino acid substitutions clustered in four hydrophobic, presumably membrane-spanning segments, that together make up only one-third of the length of the polypeptide chain. In contrast, eight mutations (5 dominant), each causing only slight impairment of function (slow alleles), were sequenced and found to specify amino acid substitutions in three hydrophilic domains. The clustering of the mutations provides independent support for the suggestion that MotA is a transmembrane proton channel and places significant constraints on models for the molecular mechanism of ion conduction.</ce:simple-para>
</ce:abstract-sec>
</ce:abstract>
<ce:keywords class="keyword" xml:lang="en"><ce:section-title>Keywords</ce:section-title>
<ce:keyword><ce:text>bacterial motility</ce:text>
</ce:keyword>
<ce:keyword><ce:text>flagellar rotation</ce:text>
</ce:keyword>
<ce:keyword><ce:text>membrane proteins</ce:text>
</ce:keyword>
<ce:keyword><ce:text>ion channels</ce:text>
</ce:keyword>
<ce:keyword><ce:text>random mutagenesis</ce:text>
</ce:keyword>
</ce:keywords>
<ce:keywords class="abr"><ce:keyword><ce:text>PMSF</ce:text>
<ce:keyword><ce:text>phenylmethylsulphonyl fluoride</ce:text>
</ce:keyword>
</ce:keyword>
<ce:keyword><ce:text>bR</ce:text>
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</head>
<tail><ce:bibliography><ce:section-title>Reference</ce:section-title>
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<ce:bib-reference id="bib5"><ce:label>Blair and Berg, 1990</ce:label>
<sb:reference><sb:contribution><sb:authors><sb:author><ce:surname>Blair</ce:surname>
<ce:given-name>D.F.</ce:given-name>
</sb:author>
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<ce:given-name>H.C.</ce:given-name>
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</sb:authors>
<sb:title><sb:maintitle>The MotA protein of <ce:italic>Escherichia coli</ce:italic>
 is a proton-conducting component of the flagellar motor</sb:maintitle>
</sb:title>
</sb:contribution>
<sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Cell</sb:maintitle>
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<sb:reference><sb:contribution><sb:authors><sb:author><ce:surname>Braiman</ce:surname>
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</sb:author>
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<ce:given-name>T.</ce:given-name>
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<mods version="3.6"><titleInfo lang="en"><title>Mutations in the MotA protein of Escherichia coli reveal domains critical for proton conduction</title>
</titleInfo>
<titleInfo type="alternative" lang="en" contentType="CDATA"><title>Mutations in the MotA protein of</title>
</titleInfo>
<name type="personal"><namePart type="given">David F.</namePart>
<namePart type="family">Blair</namePart>
<affiliation>Department of Cellular and Developmental Biology, Harvard University 16 Divinity Avenue, Cambridge, MA 02138 USA</affiliation>
<description>Present address: Department of Biology, University of Utah, Salt Lake City, Utah 84112, USA</description>
<role><roleTerm type="text">author</roleTerm>
</role>
</name>
<name type="personal"><namePart type="given">Howard C.</namePart>
<namePart type="family">Berg</namePart>
<affiliation>Department of Cellular and Developmental Biology, Harvard University 16 Divinity Avenue, Cambridge, MA 02138 USA</affiliation>
<role><roleTerm type="text">author</roleTerm>
</role>
</name>
<typeOfResource>text</typeOfResource>
<genre type="research-article">Full-length article</genre>
<originInfo><publisher>ELSEVIER</publisher>
<dateIssued encoding="w3cdtf">1991</dateIssued>
<dateValid encoding="w3cdtf">1991-07-02</dateValid>
<copyrightDate encoding="w3cdtf">1991</copyrightDate>
</originInfo>
<language><languageTerm type="code" authority="iso639-2b">eng</languageTerm>
<languageTerm type="code" authority="rfc3066">en</languageTerm>
</language>
<physicalDescription><internetMediaType>text/html</internetMediaType>
</physicalDescription>
<abstract lang="en">The MotA protein of Escherichia coli is an essential component of the torque-generating units that drive the flagellar rotary motor. A variety of evidence indicates that MotA is involved in transmembrane proton conduction. We have now mapped a number of MotA mutants, focusing primarily on those previously shown to be dominant. Fifty-six mutations (all dominant), each causing severe or complete impairment of function, were sequenced and found to correspond to 31 different alleles. All except two of these encoded amino acid substitutions clustered in four hydrophobic, presumably membrane-spanning segments, that together make up only one-third of the length of the polypeptide chain. In contrast, eight mutations (5 dominant), each causing only slight impairment of function (slow alleles), were sequenced and found to specify amino acid substitutions in three hydrophilic domains. The clustering of the mutations provides independent support for the suggestion that MotA is a transmembrane proton channel and places significant constraints on models for the molecular mechanism of ion conduction.</abstract>
<note>This work was supported by NSF grant DCB-8903690.</note>
<note type="content">Section title: Article</note>
<subject lang="en"><genre>Keywords</genre>
<topic>bacterial motility</topic>
<topic>flagellar rotation</topic>
<topic>membrane proteins</topic>
<topic>ion channels</topic>
<topic>random mutagenesis</topic>
</subject>
<subject lang="en"><topic>PMSF : phenylmethylsulphonyl fluoride</topic>
<topic>bR : bacteriorhodopsin</topic>
</subject>
<relatedItem type="host"><titleInfo><title>Journal of Molecular Biology</title>
</titleInfo>
<titleInfo type="abbreviated"><title>YJMBI</title>
</titleInfo>
<originInfo><dateIssued encoding="w3cdtf">19911020</dateIssued>
</originInfo>
<identifier type="ISSN">0022-2836</identifier>
<identifier type="PII">S0022-2836(00)X1899-2</identifier>
<part><detail type="volume"><number>221</number>
<caption>vol.</caption>
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Mutations in the MotA protein of Escherichia coli reveal domains critical for proton conduction

Mutations in the MotA protein of Escherichia coli reveal domains critical for proton conduction

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