scholarly journals Dynamics of bacterial cell division: Z ring condensation is essential for cytokinesis

2020 ◽  
Author(s):  
Georgia R. Squyres ◽  
Matthew J. Holmes ◽  
Sarah R. Barger ◽  
Betheney R. Pennycook ◽  
Joel Ryan ◽  
...  
Keyword(s):  
Cell Wall ◽  
Cell Division ◽  
Bacterial Cell ◽  
Bacterial Cell Division ◽  
Dynamic Characterization ◽  
Filament Dynamics ◽  
Division Site ◽  
Z Ring ◽  
Ring Condensation

AbstractHow proteins in the bacterial cell division complex (the divisome) coordinate to divide bacteria remains unknown. To explore how these proteins collectively function, we conducted a complete dynamic characterization of the proteins involved, and then examined the function of FtsZ binding proteins (ZBPs) and their role in cytokinesis. We find that the divisome consists of two dynamically distinct subcomplexes: stationary ZBPs that transiently bind to treadmilling FtsZ filaments, and a directionally-moving complex that includes cell wall synthases. FtsZ filaments treadmill at steady state and the ZBPs have no effect on filament dynamics. Rather, ZBPs bundle FtsZ filaments, condensing them into Z rings. Z ring condensation increases the recruitment of cell wall synthesis enzymes to the division site, and this condensation is necessary for cytokinesis.

scholarly journals Cooperative ordering of treadmilling filaments in cytoskeletal networks of FtsZ and its crosslinker ZapA

2019 ◽  
Vol 10 (1) ◽  
Author(s):  
Paulo Caldas ◽  
Mar López-Pelegrín ◽  
Daniel J. G. Pearce ◽  
Nazmi Burak Budanur ◽  
Jan Brugués ◽  
...  
Keyword(s):  
Cell Division ◽  
Bacterial Cell ◽  
Large Scale ◽  
Bacterial Cell Division ◽  
Division Site ◽  
Associated Proteins ◽  
Z Ring ◽  
Cytoskeletal Networks ◽  
Cooperative Ordering

AbstractDuring bacterial cell division, the tubulin-homolog FtsZ forms a ring-like structure at the center of the cell. This Z-ring not only organizes the division machinery, but treadmilling of FtsZ filaments was also found to play a key role in distributing proteins at the division site. What regulates the architecture, dynamics and stability of the Z-ring is currently unknown, but FtsZ-associated proteins are known to play an important role. Here, using an in vitro reconstitution approach, we studied how the well-conserved protein ZapA affects FtsZ treadmilling and filament organization into large-scale patterns. Using high-resolution fluorescence microscopy and quantitative image analysis, we found that ZapA cooperatively increases the spatial order of the filament network, but binds only transiently to FtsZ filaments and has no effect on filament length and treadmilling velocity. Together, our data provides a model for how FtsZ-associated proteins can increase the precision and stability of the bacterial cell division machinery in a switch-like manner.

scholarly journals Z-ring membrane anchors associate with cell wall synthases to initiate bacterial cell division

2018 ◽  
Vol 9 (1) ◽  
Author(s):  
Manuel Pazos ◽  
Katharina Peters ◽  
Mercedes Casanova ◽  
Pilar Palacios ◽  
Michael VanNieuwenhze ◽  
...  
Keyword(s):  
Cell Wall ◽  
Cell Division ◽  
Bacterial Cell ◽  
Bacterial Cell Division ◽  
Z Ring

scholarly journals FtsZ assembles the bacterial cell division machinery by a diffusion-and-capture mechanism

2018 ◽  
Author(s):  
Natalia Baranova ◽  
Philipp Radler ◽  
Víctor M. Hernández-Rocamora ◽  
Carlos Alfonso ◽  
Mar López-Pelegrín ◽  
...  
Keyword(s):  
Cell Division ◽  
Bacterial Cell ◽  
Bacterial Cell Division ◽  
Peptidoglycan Synthesis ◽  
Division Site ◽  
Spatiotemporal Information ◽  
Capture Mechanism ◽  
Z Ring ◽  
Membrane Bound ◽  
Transient Interactions

AbstractThe mechanism of bacterial cell division is largely unknown. The protein machinery performing cell division is organized by FtsZ, a tubulin-homolog that forms treadmilling filaments at the cell division site. Treadmilling is thought to actively move proteins around the cell thereby distributing peptidoglycan synthesis to make two new cell poles. To understand this process, we reconstituted part of the bacterial cell division machinery using the purified components FtsZ, FtsA and truncated transmembrane proteins essential for cell division. We found that membrane-bound cytosolic peptides of FtsN and FtsQ co-migrated with treadmilling FtsZ-FtsA filaments. Remarkably, rather than moving in a directed fashion, individual peptides followed FtsZ filaments by a diffusion-and-capture mechanism. Our work provides a mechanism for how the Z-ring dynamically recruits divisome proteins and highlights the importance of transient interactions for the self-organization of complex biological structures. We propose that this mechanism is used more widely to organize and transmit spatiotemporal information in living cells.One Sentence SummaryFtsZ treadmilling assembles bacterial division machinery by diffusion-and-capture mechanism.

scholarly journals Publisher Correction: Z-ring membrane anchors associate with cell wall synthases to initiate bacterial cell division

2019 ◽  
Vol 10 (1) ◽  
Author(s):  
Manuel Pazos ◽  
Katharina Peters ◽  
Mercedes Casanova ◽  
Pilar Palacios ◽  
Michael VanNieuwenhze ◽  
...  
Keyword(s):  
Cell Wall ◽  
Cell Division ◽  
Bacterial Cell ◽  
Bacterial Cell Division ◽  
Z Ring

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.

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 Lateral interactions between protofilaments of the bacterial tubulin homolog FtsZ are essential for cell division

eLife ◽  
2018 ◽  
Vol 7 ◽  
Author(s):  
Fenghui Guan ◽  
Jiayu Yu ◽  
Jie Yu ◽  
Yang Liu ◽  
Ying Li ◽  
...  
Keyword(s):  
Cell Division ◽  
Bacterial Cell ◽  
Dynamic Structure ◽  
Living Cells ◽  
Lateral Interactions ◽  
Bacterial Cell Division ◽  
Z Ring ◽  
Crystallographic Structures ◽  
Order Structures

The prokaryotic tubulin homolog FtsZ polymerizes into protofilaments, which further assemble into higher-order structures at future division sites to form the Z-ring, a dynamic structure essential for bacterial cell division. The precise nature of interactions between FtsZ protofilaments that organize the Z-ring and their physiological significance remain enigmatic. In this study, we solved two crystallographic structures of a pair of FtsZ protofilaments, and demonstrated that they assemble in an antiparallel manner through the formation of two different inter-protofilament lateral interfaces. Our in vivo photocrosslinking studies confirmed that such lateral interactions occur in living cells, and disruption of the lateral interactions rendered cells unable to divide. The inherently weak lateral interactions enable FtsZ protofilaments to self-organize into a dynamic Z-ring. These results have fundamental implications for our understanding of bacterial cell division and for developing antibiotics that target this key process.

Z Ring as Executor of Bacterial Cell Division

2006 ◽  
Vol 11 (3-5) ◽  
pp. 140-151 ◽  
Author(s):  
Alex Dajkovic ◽  
Joe Lutkenhaus
Keyword(s):  
Cell Division ◽  
Bacterial Cell ◽  
Bacterial Cell Division ◽  
Z Ring

scholarly journals Modification of cell wall polysaccharide spatially controls cell division in Streptococcus mutans

2020 ◽  
Author(s):  
Svetlana Zamakhaeva ◽  
Catherine T. Chaton ◽  
Jeffrey S. Rush ◽  
Sowmya Ajay Castro ◽  
Alexander E. Yarawsky ◽  
...  
Keyword(s):  
Cell Wall ◽  
Cell Division ◽  
Streptococcus Mutans ◽  
Cell Separation ◽  
Ring Structure ◽  
Cell Wall Polysaccharide ◽  
Bacterial Cell Division ◽  
Glycerol Phosphate ◽  
Immature Form ◽  
Z Ring

AbstractBacterial cell division is driven by a tubulin homolog FtsZ, which assembles into the Z-ring structure leading to the recruitment of the cell division machinery. In ovoid-shaped Gram-positive bacteria, such as streptococci, MapZ guides Z-ring positioning at cell equators through an, as yet, unknown mechanism. The cell wall of the important dental pathogen Streptococcus mutans is composed of peptidoglycan decorated with Serotype c Carbohydrates (SCCs). Here, we show that an immature form of SCC, lacking the recently identified glycerol phosphate (GroP) modification, coordinates Z-ring positioning. Pulldown assays using S. mutans cell wall combined with binding affinity analysis identified the major cell separation autolysin, AtlA, as an SCC binding protein. Importantly, AtlA binding to mature SCC is attenuated due to GroP modification. Using fluorescently-labeled AtlA, we mapped SCC distribution on the streptococcal surface to reveal that GroP-deficient immature SCCs are exclusively present at the cell poles and equators. Moreover, the equatorial GroP-deficient SCCs co-localize with MapZ throughout the S. mutans cell cycle. Consequently, in GroP-deficient mutant bacteria, proper AtlA localization is abrogated resulting in dysregulated cellular autolysis. In addition, these mutants display morphological abnormalities associated with MapZ mislocalization leading to Z-ring misplacement. Altogether, our data support a model in which GroP-deficient immature SCCs spatially coordinate the localization of AtlA and MapZ. This mechanism ensures cell separation by AtlA at poles and Z-ring alignment with the cell equator.Graphical abstract

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