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      Bacterial FtsZ protein forms phase‐separated condensates with its nucleoid‐associated inhibitor SlmA

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      https://www.riss.kr/link?id=O119053198

      • 저자
      • 발행기관
      • 학술지명
      • 권호사항
      • 발행연도

        2019년

      • 작성언어

        -

      • Print ISSN

        1469-221X

      • Online ISSN

        1469-3178

      • 등재정보

        SCI;SCIE;SCOPUS

      • 자료형태

        학술저널

      • 수록면

        n/a-n/a   [※수록면이 p5 이하이면, Review, Columns, Editor's Note, Abstract 등일 경우가 있습니다.]

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      다국어 초록 (Multilingual Abstract)

      Macromolecular condensation resulting from biologically regulated liquid–liquid phase separation is emerging as a mechanism to organize intracellular space in eukaryotes, with broad implications for cell physiology and pathology. Despite their small size, bacterial cells are also organized by proteins such as FtsZ, a tubulin homolog that assembles into a ring structure precisely at the cell midpoint and is required for cytokinesis. Here, we demonstrate that FtsZ can form crowding‐induced condensates, reminiscent of those observed for eukaryotic proteins. Formation of these FtsZ‐rich droplets occurs when FtsZ is bound to SlmA, a spatial regulator of FtsZ that antagonizes polymerization, while also binding to specific sites on chromosomal DNA. The resulting condensates are dynamic, allowing FtsZ to undergo GTP‐driven assembly to form protein fibers. They are sensitive to compartmentalization and to the presence of a membrane boundary in cell mimetic systems. This is a novel example of a bacterial nucleoprotein complex exhibiting condensation into liquid droplets, suggesting that phase separation may also play a functional role in the spatiotemporal organization of essential bacterial processes.










      Elements of the bacterial cell division machinery assemble into condensates by liquid‐liquid phase separation in cell‐like crowded conditions. This suggests that phase‐separated condensation may also help to organize intracellular space in bacteria.



      The essential bacterial cell division protein FtsZ forms phase‐separated condensates in the presence of nucleoprotein complexes organized by the FtsZ spatial regulator SlmA.

      The condensates are dynamic and disband upon GTP‐dependent reversible formation of FtsZ fibers whose lifetimes are significantly shortened by SlmA.

      Condensates are observed in cell‐like crowding conditions in solution and inside phase‐separated systems encircled by a lipid membrane.

      Phase‐separated FtsZ condensates may constitute a novel element of spatiotemporal organization of essential bacterial cell cycle processes.


      Elements of the bacterial cell division machinery assemble into condensates by liquid‐liquid phase separation in cell‐like crowded conditions. This suggests that phase‐separated condensation may also help to organize intracellular space in bacteria.
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      Macromolecular condensation resulting from biologically regulated liquid–liquid phase separation is emerging as a mechanism to organize intracellular space in eukaryotes, with broad implications for cell physiology and pathology. Despite their small...

      Macromolecular condensation resulting from biologically regulated liquid–liquid phase separation is emerging as a mechanism to organize intracellular space in eukaryotes, with broad implications for cell physiology and pathology. Despite their small size, bacterial cells are also organized by proteins such as FtsZ, a tubulin homolog that assembles into a ring structure precisely at the cell midpoint and is required for cytokinesis. Here, we demonstrate that FtsZ can form crowding‐induced condensates, reminiscent of those observed for eukaryotic proteins. Formation of these FtsZ‐rich droplets occurs when FtsZ is bound to SlmA, a spatial regulator of FtsZ that antagonizes polymerization, while also binding to specific sites on chromosomal DNA. The resulting condensates are dynamic, allowing FtsZ to undergo GTP‐driven assembly to form protein fibers. They are sensitive to compartmentalization and to the presence of a membrane boundary in cell mimetic systems. This is a novel example of a bacterial nucleoprotein complex exhibiting condensation into liquid droplets, suggesting that phase separation may also play a functional role in the spatiotemporal organization of essential bacterial processes.










      Elements of the bacterial cell division machinery assemble into condensates by liquid‐liquid phase separation in cell‐like crowded conditions. This suggests that phase‐separated condensation may also help to organize intracellular space in bacteria.



      The essential bacterial cell division protein FtsZ forms phase‐separated condensates in the presence of nucleoprotein complexes organized by the FtsZ spatial regulator SlmA.

      The condensates are dynamic and disband upon GTP‐dependent reversible formation of FtsZ fibers whose lifetimes are significantly shortened by SlmA.

      Condensates are observed in cell‐like crowding conditions in solution and inside phase‐separated systems encircled by a lipid membrane.

      Phase‐separated FtsZ condensates may constitute a novel element of spatiotemporal organization of essential bacterial cell cycle processes.


      Elements of the bacterial cell division machinery assemble into condensates by liquid‐liquid phase separation in cell‐like crowded conditions. This suggests that phase‐separated condensation may also help to organize intracellular space in bacteria.

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