title: Microenvironments created by liquid-liquid phase transition control the dynamic distribution of bacterial division FtsZ protein.
abstract: The influence of membrane-free microcompartments resulting from crowding-induced liquid/liquid phase separation (LLPS) on the dynamic spatial organization of FtsZ, the main component of the bacterial division machinery, has been studied using several LLPS systems. The GTP-dependent assembly cycle of FtsZ is thought to be crucial for the formation of the septal ring, which is highly regulated in time and space. We found that FtsZ accumulates in one of the phases and/or at the interface, depending on the system composition and on the oligomerization state of the protein. These results were observed both in bulk LLPS and in lipid-stabilized, phase-separated aqueous microdroplets. The visualization of the droplets revealed that both the location and structural arrangement of FtsZ filaments is determined by the nature of the LLPS. Relocation upon depolymerization of the dynamic filaments suggests the protein may shift among microenvironments in response to changes in its association state. The existence of these dynamic compartments driven by phase transitions can alter the local composition and reactivity of FtsZ during its life cycle acting as a nonspecific modulating factor of cell function.
authors.affiliation: Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas (CSIC), 28040, Madrid, Spain.
authors.forename: Begoña
authors.initials: B
authors.lastname: Monterroso
authors.affiliation: Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas (CSIC), 28040, Madrid, Spain.
authors.forename: Silvia
authors.initials: S
authors.lastname: Zorrilla
authors.affiliation: Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas (CSIC), 28040, Madrid, Spain.
authors.forename: Marta
authors.initials: M
authors.lastname: Sobrinos-Sanguino
authors.affiliation: Department of Chemistry, Pennsylvania State University, University Park, Pennsylvania 16802, USA.
authors.forename: Christine D
authors.initials: CD
authors.lastname: Keating
authors.affiliation: Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas (CSIC), 28040, Madrid, Spain.
authors.forename: Germán
authors.initials: G
authors.lastname: Rivas
mesh_terms: D001426:Bacterial Proteins / Q000378:metabolism*; D003593:Cytoplasm / Q000737:chemistry*; D003598:Cytoskeletal Proteins / Q000378:metabolism*; D004926:Escherichia coli / Q000737:chemistry*; D006160:Guanosine Triphosphate / Q000378:metabolism; D044367:Phase Transition; D055503:Protein Multimerization
chemical_list: D001426:Bacterial Proteins; D003598:Cytoskeletal Proteins; C071525:FtsZ protein, Bacteria; D006160:Guanosine Triphosphate