title: Spatiotemporal control of PopZ localization through cell cycle-coupled multimerization.
abstract: Bacterial cell poles constitute defined subcellular domains where numerous proteins localize, often at specific times, to affect various physiological processes. How pole recognition occurs and what governs the timing of protein localization are often unknown. In this paper, we investigate the mechanisms governing the localization of PopZ, a chromosome-anchoring protein whose unipolar to bipolar localization pattern is critical for cell cycle progression in Caulobacter crescentus. We provide evidence that polar localization of PopZ relied on its self-assembly into a higher-order structure (matrix) and that the unipolar to bipolar transition was coupled to the asymmetric distribution of ParA during the translocation of the origin-proximal ParB-parS partition complex. Collectively, our data suggest a model in which a local increase of ParA concentration promotes the assembly of a PopZ matrix precisely when and where this matrix is needed. Such coupling of protein assembly with a cell cycle-associated molecular asymmetry may represent a principle of cellular organization for controlling protein localization in both time and space.
authors.affiliation: Department of Molecular, Cellular and Developmental Biology, Yale University, New Haven, CT 06511, USA.
authors.forename: Géraldine
authors.initials: G
authors.lastname: Laloux
authors.forename: Christine
authors.initials: C
authors.lastname: Jacobs-Wagner
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D016935:Caulobacter crescentus / Q000166:cytology* / Q000378:metabolism*; D002453:Cell Cycle / Q000502:physiology*; D002455:Cell Division / Q000502:physiology; D016764:Cell Polarity / Q000502:physiology*; D002875:Chromosomes / Q000378:metabolism; D004926:Escherichia coli / Q000166:cytology / Q000378:metabolism; D055503:Protein Multimerization / Q000502:physiology*
chemical_list: D001426:Bacterial Proteins; C052883:chromosome partition proteins, bacterial