ArticleNature2014
MapZ marks the division sites and positions FtsZ rings in Streptococcus pneumoniae.
Article in Nature, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 126 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
126 citing papers in PubMed, 208 citations in OpenAlex.
- Structural dissection of the catalytic domain of the serine threonine kinase StkP of Streptococcus pneumoniae.Nature communications · 2026Article
- Bacterial L-forms: Key Mechanisms of Drug Resistance, Disease Recurrence, and Immune Evasion.Indian journal of microbiology · 2026Review
- Methicillin treatment reveals that FtsZ phosphorylation influences the cell division ofPNAS nexus · 2026Article
- Local peptidoglycan composition defines division site selection in Streptococcus pneumoniae.Nature microbiology · 2026Article
- Role of staphylococcal EzrA as a molecular organizer of cell division.bioRxiv : the preprint server for biology · 2026Article
- Identification of candidate nucleomodulins in ESKAPE bacteria -Frontiers in cellular and infection microbiology · 2026Article
- A modular genetic toolbox for precise gene regulation and multi-color imaging in streptococci.microLife · 2026Article
- Streptococcus pneumoniae S protein activates PBP1a to regulate peptidoglycan remodelling and cell division.Nature microbiology · 2026Article
- Epigenetic regulation of cardiac physiology and pathophysiology: biological sex matters.The journal of cardiovascular aging · 2026Article
- Tyrosine kinase Cps2C regulates the synthesis of capsular polysaccharides and plays a role in the virulence ofVirulence · 2025Article
- Amylase Binding to Oral Streptococci: A Key Interaction for Human Oral Microbial Ecology, Adaptation and Fitness.Biomolecules · 2025Review
- Milestones in the development ofJournal of bacteriology · 2025Review
- EzrA promotes Z-ring formation through interaction of its QNR motif with FtsA.Journal of bacteriology · 2025Article
- Article
- An atlas of bacterial serine-threonine kinases reveals functional diversity and key distinctions from eukaryotic kinases.Science signaling · 2025Article
- Glycosylation of serine/threonine-rich intrinsically disordered regions of membrane-associated proteins in streptococci.Nature communications · 2025Article
- How do spherical bacteria regulate cell division?Biochemical Society transactions · 2025Review
- GpsB Coordinates StkP Signaling as a PASTA Kinase Adaptor in Streptococcus pneumoniae Cell Division.Journal of molecular biology · 2024Article
- PcdA promotes orthogonal division plane selection in Staphylococcus aureus.Nature microbiology · 2024Article
- Molecular dissection of the chromosome partitioning protein RocS and regulation by phosphorylation.Journal of bacteriology · 2024Article
66 more citing papers are in PubMed but not listed here.
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Authors and funding
14 authors at 6 institutions in 5 countries.
Funding
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.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.