scholarly journals Chromosome segregation drives division site selection inStreptococcus pneumoniae

2016 ◽  
Author(s):  
Renske van Raaphorst ◽  
Morten Kjos ◽  
Jan-Willem Veening
Keyword(s):  
Cell Division ◽  
Chromosome Segregation ◽  
Site Selection ◽  
Bacterial Cell Division ◽  
Division Plane ◽  
Canonical Systems ◽  
Daughter Cells ◽  
Division Site ◽  
Additional Protein ◽  
Site Control

AbstractAccurate spatial and temporal positioning of the tubulin-like protein FtsZ is key for proper bacterial cell division.Streptococcus pneumoniae(pneumococcus) is an oval-shaped, symmetrically dividing human pathogen lacking the canonical systems for division site control (nucleoid occlusion and the Min-system). Recently, the early division protein MapZ was identified and implicated in pneumococcal division site selection. We show that MapZ is important for proper division plane selection; thus the question remains what drives pneumococcal division site selection. By mapping the cell cycle in detail, we show that directly after replication both chromosomal origin regions localize to the future cell division sites, prior to FtsZ. Perturbing the longitudinal chromosomal organization by mutating the condensin SMC, by CRISPR/Cas9-mediated chromosome cutting or by poisoning DNA decatenation resulted in mistiming of MapZ and FtsZ positioning and subsequent cell elongation. Together, we demonstrate an intimate relationship between DNA replication, chromosome segregation and division site selection in the pneumococcus, providing a simple way to ensure equally sized daughter cells without the necessity for additional protein factors.

scholarly journals Chromosome segregation drives division site selection inStreptococcus pneumoniae

2017 ◽  
Vol 114 (29) ◽  
pp. E5959-E5968 ◽  
Author(s):  
Renske van Raaphorst ◽  
Morten Kjos ◽  
Jan-Willem Veening
Keyword(s):  
Cell Division ◽  
Dna Replication ◽  
Chromosome Segregation ◽  
Site Selection ◽  
Bacterial Cell Division ◽  
Division Plane ◽  
Canonical Systems ◽  
Division Site ◽  
Z Ring ◽  
Opportunistic Human Pathogen

Accurate spatial and temporal positioning of the tubulin-like protein FtsZ is key for proper bacterial cell division.Streptococcus pneumoniae(pneumococcus) is an oval-shaped, symmetrically dividing opportunistic human pathogen lacking the canonical systems for division site control (nucleoid occlusion and the Min-system). Recently, the early division protein MapZ was identified and implicated in pneumococcal division site selection. We show that MapZ is important for proper division plane selection; thus, the question remains as to what drives pneumococcal division site selection. By mapping the cell cycle in detail, we show that directly after replication both chromosomal origin regions localize to the future cell division sites, before FtsZ. Interestingly, Z-ring formation occurs coincidently with initiation of DNA replication. Perturbing the longitudinal chromosomal organization by mutating the condensin SMC, by CRISPR/Cas9-mediated chromosome cutting, or by poisoning DNA decatenation resulted in mistiming of MapZ and FtsZ positioning and subsequent cell elongation. Together, we demonstrate an intimate relationship between DNA replication, chromosome segregation, and division site selection in the pneumococcus, providing a simple way to ensure equally sized daughter cells.

scholarly journals LocZ Is a New Cell Division Protein Involved in Proper Septum Placement in Streptococcus pneumoniae

mBio ◽  
2014 ◽  
Vol 6 (1) ◽  
Author(s):  
Nela Holečková ◽  
Linda Doubravová ◽  
Orietta Massidda ◽  
Virginie Molle ◽  
Karolína Buriánková ◽  
...  
Keyword(s):  
Cell Division ◽  
Streptococcus Pneumoniae ◽  
Protein Kinase ◽  
Bacterial Cell Division ◽  
Content Type ◽  
Daughter Cells ◽  
Division Site ◽  
Z Ring ◽  
Specific Shape ◽  
Cell Division Protein

ABSTRACTHow bacteria control proper septum placement at midcell, to guarantee the generation of identical daughter cells, is still largely unknown. Although different systems involved in the selection of the division site have been described in selected species, these do not appear to be widely conserved. Here, we report that LocZ (Spr0334), a newly identified cell division protein, is involved in proper septum placement inStreptococcus pneumoniae. We show thatlocZis not essential but that its deletion results in cell division defects and shape deformation, causing cells to divide asymmetrically and generate unequally sized, occasionally anucleated, daughter cells. LocZ has a unique localization profile. It arrives early at midcell, before FtsZ and FtsA, and leaves the septum early, apparently moving along with the equatorial rings that mark the future division sites. Consistently, cells lacking LocZ also show misplacement of the Z-ring, suggesting that it could act as a positive regulator to determine septum placement. LocZ was identified as a substrate of the Ser/Thr protein kinase StkP, which regulates cell division in S. pneumoniae. Interestingly, homologues of LocZ are found only in streptococci, lactococci, and enterococci, indicating that this close phylogenetically related group of bacteria evolved a specific solution to spatially regulate cell division.IMPORTANCEBacterial cell division is a highly ordered process regulated in time and space. Recently, we reported that the Ser/Thr protein kinase StkP regulates cell division in Streptococcus pneumoniae, through phosphorylation of several key proteins. Here, we characterized one of the StkP substrates, Spr0334, which we named LocZ. We show that LocZ is a new cell division protein important for proper septum placement and likely functions as a marker of the cell division site. Consistently, LocZ supports proper Z-ring positioning at midcell. LocZ is conserved only among streptococci, lactococci, and enterococci, which lack homologues of the Min and nucleoid occlusion effectors, indicating that these bacteria adapted a unique mechanism to find their middle, reflecting their specific shape and symmetry.

scholarly journals Cardiolipin-Containing Lipid Membranes Attract the Bacterial Cell Division Protein DivIVA

2021 ◽  
Vol 22 (15) ◽  
pp. 8350
Author(s):  
Naďa Labajová ◽  
Natalia Baranova ◽  
Miroslav Jurásek ◽  
Robert Vácha ◽  
Martin Loose ◽  
...  
Keyword(s):  
Cell Division ◽  
Lipid Bilayers ◽  
Bacterial Cell ◽  
Lipid Membranes ◽  
Model Organism ◽  
Active Role ◽  
Membrane Curvature ◽  
Bacterial Cell Division ◽  
Division Site ◽  
Clostridioides Difficile

DivIVA is a protein initially identified as a spatial regulator of cell division in the model organism Bacillus subtilis, but its homologues are present in many other Gram-positive bacteria, including Clostridia species. Besides its role as topological regulator of the Min system during bacterial cell division, DivIVA is involved in chromosome segregation during sporulation, genetic competence, and cell wall synthesis. DivIVA localizes to regions of high membrane curvature, such as the cell poles and cell division site, where it recruits distinct binding partners. Previously, it was suggested that negative curvature sensing is the main mechanism by which DivIVA binds to these specific regions. Here, we show that Clostridioides difficile DivIVA binds preferably to membranes containing negatively charged phospholipids, especially cardiolipin. Strikingly, we observed that upon binding, DivIVA modifies the lipid distribution and induces changes to lipid bilayers containing cardiolipin. Our observations indicate that DivIVA might play a more complex and so far unknown active role during the formation of the cell division septal membrane.

scholarly journals Changes in the Min Oscillation Pattern before and after Cell Birth

2010 ◽  
Vol 192 (16) ◽  
pp. 4134-4142 ◽  
Author(s):  
Jennifer R. Juarez ◽  
William Margolin
Keyword(s):  
Cell Division ◽  
Fluorescent Protein ◽  
Time Lapse ◽  
The Other ◽  
Cell Pole ◽  
Daughter Cells ◽  
Division Site ◽  
Before And After ◽  
Dividing Cells ◽  
Green Fluorescent

ABSTRACT The Min system regulates the positioning of the cell division site in many bacteria. In Escherichia coli, MinD migrates rapidly from one cell pole to the other. In conjunction with MinC, MinD helps to prevent unwanted FtsZ rings from assembling at the poles and to stabilize their positioning at midcell. Using time-lapse microscopy of growing and dividing cells expressing a gfp-minD fusion, we show that green fluorescent protein (GFP)-MinD often paused at midcell in addition to at the poles, and the frequency of midcell pausing increased as cells grew longer and cell division approached. At later stages of septum formation, GFP-MinD often paused specifically on only one side of the septum, followed by migration to the other side of the septum or to a cell pole. About the time of septum closure, this irregular pattern often switched to a transient double pole-to-pole oscillation in the daughter cells, which ultimately became a stable double oscillation. The splitting of a single MinD zone into two depends on the developing septum and is a potential mechanism to explain how MinD is distributed equitably to both daughter cells. Septal pausing of GFP-MinD did not require MinC, suggesting that MinC-FtsZ interactions do not drive MinD-septal interactions, and instead MinD recognizes a specific geometric, lipid, and/or protein target at the developing septum. Finally, we observed regular end-to-end oscillation over very short distances along the long axes of minicells, supporting the importance of geometry in MinD localization.

Differentiation of the Bacterial Cell Division Site

1989 ◽  
pp. 1-31 ◽  
Author(s):  
William R. Cook ◽  
Piet A.J. de Boer ◽  
Lawrence I. Rothfield
Keyword(s):  
Cell Division ◽  
Bacterial Cell ◽  
Bacterial Cell Division ◽  
Division Site

scholarly journals Genetic Dissection of DivIVA Functions in Listeria monocytogenes

2017 ◽  
Vol 199 (24) ◽  
Author(s):  
Karan Gautam Kaval ◽  
Samuel Hauf ◽  
Jeanine Rismondo ◽  
Birgitt Hahn ◽  
Sven Halbedel
Keyword(s):  
Cell Division ◽  
Listeria Monocytogenes ◽  
Protein Interactions ◽  
Site Selection ◽  
Genetic Dissection ◽  
Flagellar Motility ◽  
Content Type ◽  
Division Site ◽  
Interaction Partners ◽  
Species Specific

ABSTRACT DivIVA is a membrane binding protein that clusters at curved membrane regions, such as the cell poles and the membrane invaginations occurring during cell division. DivIVA proteins recruit many other proteins to these subcellular sites through direct protein-protein interactions. DivIVA-dependent functions are typically associated with cell growth and division, even though species-specific differences in the spectrum of DivIVA functions and their causative interaction partners exist. DivIVA from the Gram-positive human pathogen Listeria monocytogenes has at least three different functions. In this bacterium, DivIVA is required for precise positioning of the septum at midcell, it contributes to the secretion of autolysins required for the breakdown of peptidoglycan at the septum after the completion of cell division, and it is essential for flagellar motility. While the DivIVA interaction partners for control of division site selection are well established, the proteins connecting DivIVA with autolysin secretion or swarming motility are completely unknown. We set out to identify divIVA alleles in which these three DivIVA functions could be separated, since the question of the degree to which the three functions of L. monocytogenes DivIVA are interlinked could not be answered before. Here, we identify such alleles, and our results show that division site selection, autolysin secretion, and swarming represent three discrete pathways that are independently influenced by DivIVA. These findings provide the required basis for the identification of DivIVA interaction partners controlling autolysin secretion and swarming in the future. IMPORTANCE DivIVA of the pathogenic bacterium Listeria monocytogenes is a central scaffold protein that influences at least three different cellular processes, namely, cell division, protein secretion, and bacterial motility. How DivIVA coordinates these rather unrelated processes is not known. We here identify variants of L. monocytogenes DivIVA, in which these functions are separated from each other. These results have important implications for the models explaining how DivIVA interacts with other proteins.

scholarly journals Assembly of bacterial cell division protein FtsZ into dynamic biomolecular condensates

2020 ◽  
Author(s):  
Miguel Ángel Robles-Ramos ◽  
Silvia Zorrilla ◽  
Carlos Alfonso ◽  
William Margolin ◽  
Germán Rivas ◽  
...  
Keyword(s):  
Cell Division ◽  
Bacterial Cell ◽  
Bound State ◽  
Bacterial Cell Division ◽  
Structural Element ◽  
Physiological Factors ◽  
General Role ◽  
E Coli ◽  
Division Site ◽  
Synthetic Cell

Biomolecular condensation through phase separation may be a novel mechanism to regulate bacterial processes, including cell division. Previous work revealed FtsZ, a protein essential for cytokinesis in most bacteria, and the E. coli division site selection factor SlmA form FtsZ∙SlmA biomolecular condensates. The absence of condensates composed solely of FtsZ under the conditions used in that study suggested this mechanism was restricted to nucleoid occlusion or SlmA-containing bacteria. Here we report that FtsZ alone can demix into condensates in bulk and when encapsulated in synthetic cell-like systems. Condensate assembly depends on FtsZ being in the GDP-bound state and on crowding conditions that promote its oligomerization. FtsZ condensates are dynamic and gradually convert into FtsZ filaments upon GTP addition. Notably, FtsZ lacking its C-terminal disordered region, a structural element likely to favor biomolecular condensation, also forms condensates, albeit less efficiently. The inherent tendency of FtsZ to form condensates susceptible to modulation by physiological factors, including binding partners, suggests that such mechanisms may play a more general role in bacterial cell division than initially envisioned.

scholarly journals ZapA tetramerization is required for midcell localization and ZapB interaction in Escherichia coli

2019 ◽  
Author(s):  
Nils Y. Meiresonne ◽  
Tanneke den Blaauwen
Keyword(s):  
Cell Division ◽  
Chromosome Segregation ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Bacterial Cell Division ◽  
Cellular Processes ◽  
Interaction Partners ◽  
Associated Proteins

AbstractBacterial cell division is guided by FtsZ treadmilling precisely at midcell. FtsZ itself is regulated by FtsZ associated proteins (Zaps) that couple it to different cellular processes. ZapA is known to enhance FtsZ bundling but also forms the synchronizing link with chromosome segregation through ZapB and matS bound MatP. ZapA exists as dimers and tetramers in the cell. Using the ZapAI83E mutant that only forms dimers, this paper investigates the effects of ZapA multimerization state on its interaction partners and cell division. By employing (fluorescence) microscopy and Förster Resonance Energy Transfer in vivo it is shown that; dimeric ZapA is unable to complement a zapA deletion strain and localizes diffusely through the cell but still interacts with FtsZ that is not part of the cell division machinery. Dimeric ZapA is unable to recruit ZapB, which localizes in its presence unipolarly in the cell. Interestingly, the localization profiles of the chromosome and unipolar ZapB anticorrelate. The work presented here confirms previously reported in vitro effects of ZapA multimerization in vivo and further places it in a broader context by revealing the strong implications for ZapB localization and ter linkage.

scholarly journals Asymmetric localization of the cell division machinery during Bacillus subtilis sporulation

2020 ◽  
Author(s):  
Kanika Khanna ◽  
Javier López-Garrido ◽  
Joseph Sugie ◽  
Kit Pogliano ◽  
Elizabeth Villa
Keyword(s):  
Bacillus Subtilis ◽  
Cell Division ◽  
Vegetative Growth ◽  
Bacterial Cell ◽  
Mother Cell ◽  
Electron Tomography ◽  
Leading Edge ◽  
Specific Protein ◽  
Bacterial Cell Division ◽  
Division Plane

The mechanistic details of bacterial cell division are poorly understood. The Gram-positive bacterium Bacillus subtilis can divide via two modes. During vegetative growth, the division septum is formed at the mid cell to produce two equal daughter cells. However, during sporulation, the division septum is formed closer to one pole to yield a smaller forespore and a larger mother cell. We use cryo-electron tomography to visualize the architectural differences in the organization of FtsAZ filaments, the major orchestrators of bacterial cell division during these conditions. We demonstrate that during vegetative growth, FtsAZ filaments are present uniformly around the leading edge of the invaginating septum but during sporulation, they are only present on the mother cell side. Our data show that the sporulation septum is thinner than the vegetative septum during constriction, and that this correlates with half as many FtsZ filaments tracking the division plane during sporulation as compared to vegetative growth. We further find that a sporulation-specific protein, SpoIIE, regulates divisome localization and septal thickness during sporulation. Our data provide first evidence of asymmetric localization of the cell division machinery, and not just septum formation, to produce different cell types with diverse fates in bacteria.

scholarly journals Recombination and chromosome segregation

2004 ◽  
Vol 359 (1441) ◽  
pp. 61-69 ◽  
Author(s):  
David J. Sherratt ◽  
Britta Søballe ◽  
François–Xavier Barre ◽  
Sergio Filipe ◽  
Ivy Lau ◽  
...  
Keyword(s):  
Cell Division ◽  
Homologous Recombination ◽  
Chromosome Segregation ◽  
Atp Hydrolysis ◽  
Daughter Cells ◽  
Recombination Proteins ◽  
Recombination System ◽  
Associated Proteins ◽  
Stalled Replication Forks ◽  
Circular Chromosomes

The duplication of DNA and faithful segregation of newly replicated chromosomes at cell division is frequently dependent on recombinational processes. The rebuilding of broken or stalled replication forks is universally dependent on homologous recombination proteins. In bacteria with circular chromosomes, crossing over by homologous recombination can generate dimeric chromosomes, which cannot be segregated to daughter cells unless they are converted to monomers before cell division by the conserved Xer site–specific recombination system. Dimer resolution also requires FtsK, a division septum–located protein, which coordinates chromosome segregation with cell division, and uses the energy of ATP hydrolysis to activate the dimer resolution reaction. FtsK can also translocate DNA, facilitate synapsis of sister chromosomes and minimize entanglement and catenation of newly replicated sister chromosomes. The visualization of the replication/recombination–associated proteins, RecQ and RarA, and specific genes within living Escherichia coli cells, reveals further aspects of the processes that link replication with recombination, chromosome segregation and cell division, and provides new insight into how these may be coordinated.

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