Polar localization of the MinD protein of Bacillus subtilis and its role in selection of the mid-cell division site

Adele L Marston, Helena B. Thomaides, David H. Edwards, Michaela E. Sharpe, Jeffery Errington

    Research output: Contribution to journalArticle

    262 Citations (Scopus)

    Abstract

    Cell division in rod-shaped bacteria is initiated by formation of a ring of the tubulin-like protein FtsZ at mid-cell. Division site selection is controlled by a conserved division inhibitor MinCD, which prevents aberrant division at the cell poles. The Bacillus subtilis DivIVA protein controls the topological specificity of MinCD action. Here we show that DivIVA is targeted to division sites late in their assembly, after some MinCD-sensitive step requiring FtsZ and other division proteins has been passed. DivIVA then recruits MinD to the division sites preventing another division from taking place near the newly formed cell poles. Sequestration of MinD to the poles also releases the next mid-cell sites for division. Remarkably, this mechanism of DivIVA action is completely different from that of the equivalent protein MinE of Escherichia coli, even though both systems operate via the same division inhibitor MinCD.
    Original languageEnglish
    Pages (from-to)3419-3430
    Number of pages12
    JournalGenes & Development
    Volume12
    Issue number21
    Publication statusPublished - 1 Nov 1998

    Fingerprint

    Bacillus subtilis
    Cell Division
    Proteins
    Escherichia coli Proteins
    Tubulin
    Bacteria

    Keywords

    • Bacillus subtilis
    • DivIVA
    • Cell division
    • MinD
    • Cytokinesis

    Cite this

    Marston, Adele L ; Thomaides, Helena B. ; Edwards, David H. ; Sharpe, Michaela E. ; Errington, Jeffery. / Polar localization of the MinD protein of Bacillus subtilis and its role in selection of the mid-cell division site. In: Genes & Development. 1998 ; Vol. 12, No. 21. pp. 3419-3430.
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    abstract = "Cell division in rod-shaped bacteria is initiated by formation of a ring of the tubulin-like protein FtsZ at mid-cell. Division site selection is controlled by a conserved division inhibitor MinCD, which prevents aberrant division at the cell poles. The Bacillus subtilis DivIVA protein controls the topological specificity of MinCD action. Here we show that DivIVA is targeted to division sites late in their assembly, after some MinCD-sensitive step requiring FtsZ and other division proteins has been passed. DivIVA then recruits MinD to the division sites preventing another division from taking place near the newly formed cell poles. Sequestration of MinD to the poles also releases the next mid-cell sites for division. Remarkably, this mechanism of DivIVA action is completely different from that of the equivalent protein MinE of Escherichia coli, even though both systems operate via the same division inhibitor MinCD.",
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    author = "Marston, {Adele L} and Thomaides, {Helena B.} and Edwards, {David H.} and Sharpe, {Michaela E.} and Jeffery Errington",
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    Polar localization of the MinD protein of Bacillus subtilis and its role in selection of the mid-cell division site. / Marston, Adele L; Thomaides, Helena B.; Edwards, David H.; Sharpe, Michaela E.; Errington, Jeffery.

    In: Genes & Development, Vol. 12, No. 21, 01.11.1998, p. 3419-3430.

    Research output: Contribution to journalArticle

    TY - JOUR

    T1 - Polar localization of the MinD protein of Bacillus subtilis and its role in selection of the mid-cell division site

    AU - Marston, Adele L

    AU - Thomaides, Helena B.

    AU - Edwards, David H.

    AU - Sharpe, Michaela E.

    AU - Errington, Jeffery

    PY - 1998/11/1

    Y1 - 1998/11/1

    N2 - Cell division in rod-shaped bacteria is initiated by formation of a ring of the tubulin-like protein FtsZ at mid-cell. Division site selection is controlled by a conserved division inhibitor MinCD, which prevents aberrant division at the cell poles. The Bacillus subtilis DivIVA protein controls the topological specificity of MinCD action. Here we show that DivIVA is targeted to division sites late in their assembly, after some MinCD-sensitive step requiring FtsZ and other division proteins has been passed. DivIVA then recruits MinD to the division sites preventing another division from taking place near the newly formed cell poles. Sequestration of MinD to the poles also releases the next mid-cell sites for division. Remarkably, this mechanism of DivIVA action is completely different from that of the equivalent protein MinE of Escherichia coli, even though both systems operate via the same division inhibitor MinCD.

    AB - Cell division in rod-shaped bacteria is initiated by formation of a ring of the tubulin-like protein FtsZ at mid-cell. Division site selection is controlled by a conserved division inhibitor MinCD, which prevents aberrant division at the cell poles. The Bacillus subtilis DivIVA protein controls the topological specificity of MinCD action. Here we show that DivIVA is targeted to division sites late in their assembly, after some MinCD-sensitive step requiring FtsZ and other division proteins has been passed. DivIVA then recruits MinD to the division sites preventing another division from taking place near the newly formed cell poles. Sequestration of MinD to the poles also releases the next mid-cell sites for division. Remarkably, this mechanism of DivIVA action is completely different from that of the equivalent protein MinE of Escherichia coli, even though both systems operate via the same division inhibitor MinCD.

    KW - Bacillus subtilis

    KW - DivIVA

    KW - Cell division

    KW - MinD

    KW - Cytokinesis

    M3 - Article

    VL - 12

    SP - 3419

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    JO - Genes & Development

    JF - Genes & Development

    SN - 0890-9369

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    ER -