Mutations in the MotA protein of Escherichia coli reveal domains critical for proton conduction
Identifieur interne : 001666 ( Main/Exploration ); précédent : 001665; suivant : 001667Mutations in the MotA protein of Escherichia coli reveal domains critical for proton conduction
Auteurs : David F. Blair [États-Unis] ; Howard C. Berg [États-Unis]Source :
- Journal of Molecular Biology [ 0022-2836 ] ; 1991.
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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.
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DOI: 10.1016/0022-2836(91)90943-Z
Affiliations:
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Blair</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Massachusetts</region></placeName><wicri:cityArea>Department of Cellular and Developmental Biology, Harvard University 16 Divinity Avenue, Cambridge</wicri:cityArea></affiliation></author><author><name sortKey="Berg, Howard C" sort="Berg, Howard C" uniqKey="Berg H" first="Howard C." last="Berg">Howard C. 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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></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Massachusetts</li></region></list><tree><country name="États-Unis"><region name="Massachusetts"><name sortKey="Blair, David F" sort="Blair, David F" uniqKey="Blair D" first="David F." last="Blair">David F. Blair</name></region><name sortKey="Berg, Howard C" sort="Berg, Howard C" uniqKey="Berg H" first="Howard C." last="Berg">Howard C. Berg</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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