TY - JOUR
T1 - Bacterial FtsZ protein forms phase-separated condensates with its nucleoid-associated inhibitor SlmA
AU - Monterroso, Begoña
AU - Zorrilla, Silvia
AU - Sobrinos-Sanguino, Marta
AU - Robles-Ramos, Miguel A.
AU - López-Álvarez, Marina
AU - Margolin, William
AU - Keating, Christine D.
AU - Rivas, Germán
N1 - Funding Information:
Authors thank W.T.S. Huck and A. Piruska (Radboud University, Nijmegen) for kindly providing the chips designs and silicon masters for microfluidics; N. Ropero for technical assistance in protein purification and labeling; M.T. Seis-dedos and G. Elvira (Confocal Laser and Multidimensional Microscopy Facility, CIB-CSIC) for excellent support in imaging; and the Technical Support Facility (CIB-CSIC) for invaluable input. This work was supported by the Fondo Europeo de Desarrollo Regional (FEDER) and the Agencia Estatal de Investigación (AEI); by the Spanish government (BFU2014-52070-C2-2-P and BFU2016-75471-C2-1-P, G. R.); by the National Institutes of Health (GM61074, W. M.); and by the National Science Foundation (MCB-1715984, C. D. K.). M.L.-A. was supported by the European Social Fund (ESF 2014-2020).
Funding Information:
Authors thank W.T.S. Huck and A. Piruska (Radboud University, Nijmegen) for kindly providing the chips designs and silicon masters for microfluidics; N. Ropero for technical assistance in protein purification and labeling; M.T. Seisdedos and G. Elvira (Confocal Laser and Multidimensional Microscopy Facility, CIB-CSIC) for excellent support in imaging; and the Technical Support Facility (CIB-CSIC) for invaluable input. This work was supported by the Fondo Europeo de Desarrollo Regional (FEDER) and the Agencia Estatal de Investigaci?n (AEI); by the Spanish government (BFU2014-52070-C2-2-P and BFU2016-75471-C2-1-P, G. R.); by the National Institutes of Health (GM61074, W. M.); and by the National Science Foundation (MCB-1715984, C. D. K.). M.L.-A. was supported by the European Social Fund (ESF 2014-2020).
Publisher Copyright:
© 2018 The Authors
PY - 2019/1
Y1 - 2019/1
N2 - 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.
AB - 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.
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U2 - 10.15252/embr.201845946
DO - 10.15252/embr.201845946
M3 - Article
C2 - 30523075
AN - SCOPUS:85058034622
VL - 20
JO - EMBO Reports
JF - EMBO Reports
SN - 1469-221X
IS - 1
M1 - e45946
ER -