title: MapZ marks the division sites and positions FtsZ rings in Streptococcus pneumoniae.
abstract: In every living organism, cell division requires accurate identification of the division site and placement of the division machinery. In bacteria, this process is traditionally considered to begin with the polymerization of the highly conserved tubulin-like protein FtsZ into a ring that locates precisely at mid-cell. Over the past decades, several systems have been reported to regulate the spatiotemporal assembly and placement of the FtsZ ring. However, the human pathogen Streptococcus pneumoniae, in common with many other organisms, is devoid of these canonical systems and the mechanisms of positioning the division machinery remain unknown. Here we characterize a novel factor that locates at the division site before FtsZ and guides septum positioning in pneumococcus. Mid-cell-anchored protein Z (MapZ) forms ring structures at the cell equator and moves apart as the cell elongates, therefore behaving as a permanent beacon of division sites. MapZ then positions the FtsZ ring through direct protein-protein interactions. MapZ-mediated control differs from previously described systems mostly on the basis of negative regulation of FtsZ assembly. Furthermore, MapZ is an endogenous target of the Ser/Thr kinase StkP, which was recently shown to have a central role in cytokinesis and morphogenesis of S. pneumoniae. We show that both phosphorylated and non-phosphorylated forms of MapZ are required for proper Z-ring formation and dynamics. Altogether, this work uncovers a new mechanism for bacterial cell division that is regulated by phosphorylation and illustrates that nature has evolved a diversity of cell division mechanisms adapted to the different bacterial clades.
authors.affiliation: Bases Moléculaires et Structurales des Systèmes Infectieux, IBCP, Université Lyon 1, CNRS, UMR 5086, Lyon, 69007, France.
authors.forename: Aurore
authors.initials: A
authors.lastname: Fleurie
authors.affiliation: Department of Biochemistry, University of Oxford, South parks road, OX1 3QU, United Kingdom.
authors.forename: Christian
authors.initials: C
authors.lastname: Lesterlin
authors.affiliation: Bases Moléculaires et Structurales des Systèmes Infectieux, IBCP, Université Lyon 1, CNRS, UMR 5086, Lyon, 69007, France.
authors.forename: Sylvie
authors.initials: S
authors.lastname: Manuse
authors.affiliation: Bases Moléculaires et Structurales des Systèmes Infectieux, IBCP, Université Lyon 1, CNRS, UMR 5086, Lyon, 69007, France.
authors.forename: Chao
authors.initials: C
authors.lastname: Zhao
authors.affiliation: Laboratoire de Biologie Tissulaire et d'Ingénierie Thrérapeutique, IBCP, Université Lyon 1, CNRS, UMR 5305, Lyon, 69007, France.
authors.forename: Caroline
authors.initials: C
authors.lastname: Cluzel
authors.affiliation: Bases Moléculaires et Structurales des Systèmes Infectieux, IBCP, Université Lyon 1, CNRS, UMR 5086, Lyon, 69007, France.
authors.forename: Jean-Pierre
authors.initials: JP
authors.lastname: Lavergne
authors.affiliation: Proteome Center Tübingen, University of Tübingen, Auf der Morgenstelle 15, Tuebingen, 72076, Germany.
authors.forename: Mirita
authors.initials: M
authors.lastname: Franz-Wachtel
authors.affiliation: Proteome Center Tübingen, University of Tübingen, Auf der Morgenstelle 15, Tuebingen, 72076, Germany.
authors.forename: Boris
authors.initials: B
authors.lastname: Macek
authors.affiliation: Bases Moléculaires et Structurales des Systèmes Infectieux, IBCP, Université Lyon 1, CNRS, UMR 5086, Lyon, 69007, France.
authors.forename: Christophe
authors.initials: C
authors.lastname: Combet
authors.affiliation: Departments of Biology and Chemistry, Indiana University, Bloomington, IN 47405, USA.
authors.forename: Erkin
authors.initials: E
authors.lastname: Kuru
authors.affiliation: Departments of Biology and Chemistry, Indiana University, Bloomington, IN 47405, USA.
authors.forename: Michael S
authors.initials: MS
authors.lastname: VanNieuwenhze
authors.affiliation: Departments of Biology and Chemistry, Indiana University, Bloomington, IN 47405, USA.
authors.forename: Yves V
authors.initials: YV
authors.lastname: Brun
authors.affiliation: Department of Biochemistry, University of Oxford, South parks road, OX1 3QU, United Kingdom.
authors.forename: David
authors.initials: D
authors.lastname: Sherratt
authors.affiliation: Bases Moléculaires et Structurales des Systèmes Infectieux, IBCP, Université Lyon 1, CNRS, UMR 5086, Lyon, 69007, France.
authors.forename: Christophe
authors.initials: C
authors.lastname: Grangeasse
mesh_terms: D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D048749:Cytokinesis; D003598:Cytoskeletal Proteins / Q000378:metabolism*; D010766:Phosphorylation; D021381:Protein Transport; D013296:Streptococcus pneumoniae / Q000166:cytology* / Q000378:metabolism*; D014404:Tubulin / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D003598:Cytoskeletal Proteins; C071525:FtsZ protein, Bacteria; D014404:Tubulin