Analyses of the Flagellar Filaments of the <i>Salmonella</i> Pseudorevertants

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  • HAYASHI Fumio
    Department of Chemistry and Chemical Biology, Graduate School of Engineering, Gunma University
  • TOMARU Hidetoshi
    Department of Chemistry and Chemical Biology, Graduate School of Engineering, Gunma University
  • OOSAWA Kenji
    Department of Chemistry and Chemical Biology, Graduate School of Engineering, Gunma University

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  • サルモネラ菌復帰変異体べん毛繊維のらせん構造と機能
  • サルモネラキン フッキ ヘンイタイ ベンモウ センイ ノ ラセン コウゾウ ト キノウ

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Abstract

A Salmonella cell swims by rotating its flagellar filaments. Each filament (∼10 μm) is composed of ∼30,000 molecules of a single protein flagellin and forms a left-handed helical structure under physiological conditions. The cells repeat swim-and-tumble and consequently move toward their favored environments and away from unflavored ones. The swim-and-tumble is caused by the change of the filament shape introduced by reversal of flagellar rotation. Such a change of the filament shape is called a polymorphic transformation. To elucidate the transformation mechanism of flagellar filaments, we applied genetic suppressor analysis within flagellin molecule and identified the 19 key amino acid residues contributing to the transformation. To estimate the roles of the key amino acid residues, we analyzed the shapes of the flagellar filaments and the functions (swimming and tumble activities) of the pseudorevertants, and we investigated the localization of the key amino acid residues on L- and R-type flagellin molecules. From these results, we propose a novel mechanism for the polymorphic transformation.<br>

Journal

  • KOBUNSHI RONBUNSHU

    KOBUNSHI RONBUNSHU 67 (12), 666-678, 2010

    The Society of Polymer Science, Japan

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