Publication Date:
2014-12-04
Description:
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.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4268495/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉 〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4268495/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fleurie, Aurore -- Lesterlin, Christian -- Manuse, Sylvie -- Zhao, Chao -- Cluzel, Caroline -- Lavergne, Jean-Pierre -- Franz-Wachtel, Mirita -- Macek, Boris -- Combet, Christophe -- Kuru, Erkin -- VanNieuwenhze, Michael S -- Brun, Yves V -- Sherratt, David -- Grangeasse, Christophe -- 083469/Wellcome Trust/United Kingdom -- 091911/Wellcome Trust/United Kingdom -- GM051986/GM/NIGMS NIH HHS/ -- R01 GM051986/GM/NIGMS NIH HHS/ -- WT083469MA/Wellcome Trust/United Kingdom -- England -- Nature. 2014 Dec 11;516(7530):259-62. doi: 10.1038/nature13966. Epub 2014 Nov 26.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Bases Moleculaires et Structurales des Systemes Infectieux, IBCP, Universite Lyon 1, CNRS, UMR 5086, Lyon 69007, France. ; Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK. ; Laboratoire de Biologie Tissulaire et d'Ingenierie Threrapeutique, IBCP, Universite Lyon 1, CNRS, UMR 5305, Lyon 69007, France. ; Proteome Center Tubingen, University of Tubingen, Auf der Morgenstelle 15, Tubingen 72076, Germany. ; Departments of Biology and Chemistry, Indiana University, Bloomington, Indiana 47405, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25470041" target="_blank"〉PubMed〈/a〉
Keywords:
Bacterial Proteins/genetics/*metabolism
;
*Cytokinesis
;
Cytoskeletal Proteins/*metabolism
;
Phosphorylation
;
Protein Transport
;
Streptococcus pneumoniae/*cytology/*metabolism
;
Tubulin/metabolism
Print ISSN:
0028-0836
Electronic ISSN:
1476-4687
Topics:
Biology
,
Chemistry and Pharmacology
,
Medicine
,
Natural Sciences in General
,
Physics
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