z ring formation in bacteria

J Bacteriol 2003; 185:196–203. Plant-Specific Protein MCD1 Determines the Site of ... The figure symbols are the same as those in (B). Order the following steps in cell division. Z Division‐site localization of RodZ is required ... - Wiley https://micro.cornell.edu/.../binary-fission-and-other-forms-reproduction-bacteria The MinD ATPase is a SIMIBI family member with homology to FlhG proteins (Fig. ch 7 Flashcards - Quizlet Knowing where proteins are in the cell is often critical to understanding their function. The purpose of our study is to reconstitute the chloroplast Z ring in bacteria. Abstract. RCSB PDB - 6SCS: Cell Division Protein SepF in complex ... The earliest stage of cell division in bacteria is the formation of a Z ring, composed of a polymer of the FtsZ protein, at the division site. In all studied strains, the intensity of Z-ring fluorescence increased over time (figure 4b). Ohlrogge JB, Gunstone FD, Ismail IA, Lands WE. EMB agar is a medium used in the identification and isolation of pathogenic bacteria. Bacterial Proteins and Cell Division Oscillation in Bacteria Bacterial cell division: Regulating Z-ring formation ... PubMed CrossRef Google Scholar The formation of dynamic FtsZ polymers is crucial for functional Z-ring formation in vivo. Importantly, in E. coli and B. subtilis the ring is known to form well before constriction ( … Binary Fission and other Forms of Reproduction in Bacteria ... ParA and ParB coordinate chromosome segregation with cell ... z ring The nucleoid occlusion mechanism is critical for the timing of chromosome partitioning. Together with several … Bacterial cell division occurs through the formation of an FtsZ ring (Z ring) at the site of division. The cytokinesis is followed by the formation of a cell wall if the parent cell had a cell wall and a new cell wall usually begin as a Z-ring which is formed by the cytoskeleton FtsZ. Autoinducers, receptors, and specificity. Monterroso and co-workers proposed that before Z-ring formation, binding of SlmA to SlmA-binding sequences (SBS) helps sequester FtsZ within condensates near the cell membrane, and that once the cell is ready for division, FtsZ is recruited to the midcell to polymerize into the Z-ring driven by GTP (Fig. Assembly of the cell division apparatus in bacteria starts with formation of the Z ring on the cytoplasmic face of the membrane. Cell wall-synthesizing machinery is assembled 4). 2 G; ). Formation of the Z ring 2). Bacterial cell division occurs through the formation of an FtsZ ring (Z ring) at the site of division. In many bacteria, spatial regulation of Z-ring formation is controlled by the Min system (for detailed reviews, see Barak and Wilkinson, 2007; Lutkenhaus, 2007). During cell division, FtsZ filaments assemble into a ring (Z-ring) at the site where the septum forms. The septum is one of the key cellular structures during the cell division of Gram-positive bacteria. In E. coli and B. subtilis, the positioning of the Z ring has been widely studied. Z ring formation is also stabilized by DynA and DynB, two dynamin-like proteins which interact directly with SsgB and SepF2 during division (Schlimpert et al., 2017). The ring is composed of the tubulin-like FtsZ protein that has GTPase activity and the ability to polymerize in vitro. "That is where the control is happening." The mechanisms of Z-ring assembly and regulation in bacteria are poorly understood, particularly in non-model organisms. Additional gradients of negative regulators of FtsZ assembly are used by E. coli and other bacteria to achieve spatial control of Z-ring assembly. (B) Division forms a large mother cell and two small offspring cells. The interaction of a diverse repertoire of accessory proteins with FtsZ contributes to the formation of a functional division machine that is responsive to cell cycle status and environmental stress. ... Two rings are formed near the pole of the cell out of which 1-Z ring gets activated and septum at the pole while other Z-ring dissemble. A critical event in the bacterial division process is the polymerization of the tubulin-like protein FtsZ into an annular structure called the Z ring, which locates the division site and recruits the numerous proteins required to carry out cytokinesis (Bi and Lutkenhaus, 1991; Addinall and Holland, 2002; Margolin, 2005; Harry et al., 2006). However, the properties of chloroplast FtsZs remain unclarified. A. Research into the control of Z ring positioning in … Z ring is anchored to the plasma membrane 3). Evidence suggests that the Z ring is utilized by all prokaryotic organisms for division and may also be used by some eukaryotic organelles. This review summarizes our present knowledge about the formation, function, and evolution of the Z ring in prokaryotic cell division. As a validated antimicrobial target, considerable efforts have been devoted to identify small molecule FtsZ inhibitors. Fts formation step #1. The D-phase is initiated by the FtsZ proteins, which usually distributed uniformly; assemble in form of a ring (Z-ring) at the midpoint of the cell. FtsA assists in the formation of the Z ring and also has a critical role in recruiting downstream division proteins to the Z ring to generate the divisome that divides the cell. Z-ring force and cell shape during division in rod-like bacteria Ganhui Lan*, Charles W. Wolgemuth†, and Sean X. As in bacteria, the prokaryotic tubulin homolog FtsZ assembles into a ring-like structure (Z ring) at mid-chloroplast, and this process is followed by constriction. Two pathways during cell cycle. Note 2: The self-produced matrix of extracellular polymeric substances, which is … in Caulobacter cres… Division-site localization of RodZ is required for efficient Z ring formation in Escherichia coli. Bacterial cell division occurs through the formation of an FtsZ ring (Z ring) at the site of division. This … Fts formation step #2. importantly, in bacteria (Arigoni et al. Formation of a Z ring was delayed by deletion of rodZ, suggesting that division‐site localization of RodZ facilitated the formation or stabilization of the Z ring during early cell division. In rod‐shaped bacteria, Z ring formation occurs precisely at midcell and is co‐ordinated temporally with the progress of the cell cycle. The life cycle of bacterial cells consists of repeated elongation, septum formation, and division. Robust cell proliferation requires precise coordination of key cell-cycle processes. In contrast with the timing of Z-ring formation, the timing of FtsZ fluorescence appearance was not significantly different in the hyphae of all analysed deletion strains and the wild-type (figure 4b,e, table 2). Bacteria such as Escherichia coli must coordinate cell elongation and cell division. [Google Scholar] Okuyama H, Okajima N, Sasaki S, Higashi S, Murata N. Since FtsZ is essential for cell division in bacteria, this protein is a target for the design of new antibiotics. Central to almost all bactrial division is the FtsZ protein. 3 FtsZ and the Z-ring. - tubulin homologue, found in most bacteria and archaea - polymerization forms Z ring, meshwork of filaments MinCDE system in E. coli limits the Z ring to the center of the cell 1. Understanding the mechanisms responsible for dynamics of the Z-ring is important for our understanding of cell division in prokaryotic cells.In this work, we present a minimal stochastic model that qualititatively reproduces observations of polymerization, of formation of dynamic contractile ring that is stable for a long time and of depolymerization shown by FtsZ … Instead of placing the FtsZ ring at the center of the cell, as in binary fission, (A) Z rings are placed near both cell poles in Epulopiscium. Registration No 3,257,927) and Goldbio (U.S. The cytoskeletal protein FtsZ polymerizes to form the _____ _____ that marks the site of septum formation in bacteria and archaea. MinC, MinD, MinE oscillate from one side of cell to other: high amounts of MinC at poles prevent Z ring formation at those locations 2. Before septum formation, a division ring called the Z-ring, which is made of a filamentous tubulin analog, FtsZ, is seen at the mid cell. A mother cell propagates by septum formation and subsequent septum splitting (1, 2).The septum structure and formation are closely related to the means of daughter cell separation during cell division. There currently exist several models and mechanisms that regulate Z-ring formation, but these mechanisms depend on the species. The initials FtsZ mean " F ilamenting t emperature- s ensitive mutant Z ." Chrysophaentins are competitive inhibitors of FtsZ and inhibit Z-ring formation in live bacteria. https://www.microbiologytext.com/6th_ed/book/displayarticle/834 Active chromosome segregation begins soon after the initiation of replication in the oriC region (origin of replication). Before septum formation, a divi sion ring called the Z-ring, which is made of a filamentous tubulin analog, FtsZ, is seen at the mid cell. FtsZ is a protein encoded by the ftsZ gene that assembles into a ring at the future site of bacterial cell division (also called the Z ring ). Reconstitution of the chloroplast Z ring in a bacterial cell is of great interest from the view of the evolutionary stability of the Z ring-centered division machinery. Registration No 3,257,926) are registered trademarks of Gold Biotechnology, Inc. The clustering of chemotaxis proteins plays an important The life cycle of bacterial cells consists of repeated elongation, septum formation, and division. Bacteria with mutant FtsZ gene fail to form septum and cannot divide. Fission, in biology, is the division of a single entity into two or more parts and the regeneration of those parts to separate entities resembling the original.The object experiencing fission is usually a cell, but the term may also refer to how organisms, bodies, populations, or species split into discrete parts. Elongation is regulated by an elongasome complex containing MreB actin and the transmembrane protein RodZ, which regulates assembly of MreB, whereas division is regulated by a divisome complex … Thus, the position of the aforementioned FtsZ ring (the Z-ring) dictates where cytokinesis will take place (Margolin 2005). In Escherichia coli, the Z ring recruits at least ten other proteins, all of which are required for the progression and completion of cytokinesis 2, as will be discussed below. The FtsZ protein is similar to tubulin- protein that forms contractile ring in eukaryotic cell division. Biochim Biophys Acta. A screen for compounds that inhibit disulfide bond formation in β-galactosidase in Escherichia coli found inhibitors of the membrane enzyme DsbB. Scale bar: 10 μm. FtsZ is a prokaryotic homologue of the eukaryotic protein tubulin. Sun*‡§ *Department of Mechanical Engineering and ‡Whitaker Institute of Biomedical Engineering, The Johns Hopkins University, Baltimore, MD 21218; and †Department of Cell Biology and Center for Cell Analysis and Modeling, University of Connecticut Health … FtsZ is also highly dynamic within the assembled Z-ring, with molecules in the ring turning over with a half-time of ∼10–30 s as measured by fluorescence recovery after photobleaching [4,5].Notably, the recovery time is significantly extended upon expression of a GTPase-deficient FtsZ variant, indicating a dependence of polymer dynamics on FtsZ's GTPase … Visualization of strains with GFP-labeled FtsZ shows that the Z-ring contracts before In some bacteria which lack this system, e.g., Mycobacterium tuberculosis, its absence can cause imprecise placement of the Z-ring during cell division. The chloroplast has inherited its inner division ring (Z ring) from bacteria to some extent. Set up z ring formation by Fts proteins. Scale bar: 10 μm. septum formation, and division. FtsZ (Z) interacts with the cytoplasmic cell division protein FtsA (A) via the C-terminal tail of Z, which is fl exible. ... Axial filament and Septum Formation. In the reaction with propargyl bromide, the thiazoline ring opens and subsequently closes via a [2 + 2] cycloaddition between an in situ generated allene and the α,β-unsaturated methyl ester. The Min System is a mechanism composed of three proteins MinC, MinD, and MinE used by E. coli as a means of properly localizing the septum prior to cell division.Each component participates in generating a dynamic oscillation of FtsZ protein inhibition between the two bacterial poles to precisely specify the mid-zone of the cell, allowing the cell to accurately … The spatial and temporal control of Filamenting temperature sensitive mutant Z (FtsZ) Z-ring formation is crucial for proper cell division in bacteria. Bacteria that have a coccoid morphology, such as S. aureus , have Z rings which are positioned in all planes. MreB and Determinants of Cell Morphology MreB is a … Chloroplasts evolved from a cyanobacterial endosymbiont [1, 2], and chloroplast division requires the formation of an FtsZ division ring, which is descended from the cytokinetic machinery of cyanobacteria [3–5]. In experiments conducted with an anti-FtsZ antibody and a fluorescent secondary antibody, RayChaudhuri and co-workers found that treatment of E. coli with zantrin Z1 led to a mislocalization of FtsZ to the poles of the cell rather than mid-cell, and treatment with zantrin Z3 also led to perturbations of Z-ring formation and integrity. Together with several other proteins, FtsZ is essential for cell division. 25 . The spatial and temporal control of Filamenting temperature sensitive mutant Z (FtsZ) Z-ring formation is crucial for proper cell division in bacteria. Ultimately, this ensures that the division septum forms between replicated and segregated … Because the maturation time is shorter, the ring cannot catch up with the core formation and the eventual ring width is smaller. (A and B) Formation of the Z ring and anchoring of the Z ring to the membrane. 2 G; ). The Z ring forms a rigid band attached to the peptidoglycan. Proteus spp. FtsZ (Z) interacts with the cytoplasmic cell division protein FtsA (A) via the C-terminal tail of Z, which is fl exible. The ring is composed of the tubulin-like FtsZ protein that has GTPase activity and the ability to polymerize in vitro. The Z ring is thought to function in vivo as a cytoskeletal element that is analogous to the contractile ring in many eukaryotic cells. Aggregate of microorganisms in which cells that are frequently embedded within a self-produced matrix of extracellular polymeric substances (EPSs) adhere to each other and/or to a surface.. In rod‐shaped bacteria, Z ring formation occurs precisely at midcell and is co‐ordinated temporally with the progress of the cell cycle. Sun*‡§ *Department of Mechanical Engineering and ‡Whitaker Institute of Biomedical Engineering, The Johns Hopkins University, Baltimore, MD 21218; and †Department of Cell Biology and Center for Cell Analysis and Modeling, University of Connecticut Health … The life cycle of bacterial cells consists of repeated elongation, septum formation, and division. We recently discovered the … The life cycle of bacterial cells consists of repeated elongation, septum formation, and division. Bacteria that live in heterogeneous populations presumably encounter complex mixtures of autoinducers that are produced by themselves, their clonal siblings, close relatives, and their non-kin neighbours, which could be fierce competitors 7,12,13.Thus, bacteria face the challenge of extracting information from mixtures of … Bacteria inhibit septation by synthesizing protein SulA, an FtsZ inhibitor that halts Z-ring formation, thereby stopping recruitment and activation of PBP3. (C) The smaller cells contain DNA and become fully engulfed by the larger mother cell. 1976 May 27; 431 (2):257–267. It contains digested meat proteins as a source of organic nutrients. Like tubulin, FtsZ is a GTPase and can polymerise into filaments. Given the importance of … Together with several … This results in only half of the new bacterial cells surviving, which is not so good for bacterial growth. Z-ring acts as a sort of scaffold where the complete division apparatus (the so-called divisome) is assembled. 1995). Before septum formation, a division ring called the Z-ring, which is made of a filamentous tubulin analog, FtsZ, is seen at the mid cell. During vegetative growth, the Z ring is positioned in the middle of the cell, as in E. coli, but during sporulation a Z ring is positioned at each cell pole . Positional specificity of cyclopropane ring formation from cis-octadecenoic acid isomers in Escherichia coli. of Z rings near the poles.There is evidence that other proteins,such as EzrA,affect the stability of FtsZ poly-mers to enhance Z-ring assembly only at appropriate locations.Additional proteins (such as YneA in B. sub-tilis and SulA in E. coli) destabilize Z-ring formation to prevent cell division when DNA damage is detected 20,21. The data suggest that cellular branching in E. coliis specifically induced by aberrant septation events caused by mis-oriented Z rings and not by deformation of a growing cell pole or emergence of new tips from the sidewall, which are likely mechanisms of branching in other bacterial families. Aside from its role in Z ring assembly, FtsA is now know n to affect the in tegrity of t he Z ring a t vario us sta ges of divis ome ass embly 67 ,72,74,81 . Reaction of thiazoline fused 2-pyridones with alkyl halides in the presence of cesium carbonate opens the thiazoline ring via S-alkylation and generates N-alkenyl functionalized 2-pyridones. It is directed by a protein called Ftsz B. FtsZ proteins polymerize into a Z ring on the cytoplasmic membrane C. MinCDE is responsible for a Z ring formation at the center of a cell Additional proteins are added to the Z ring to form the divisome E. D. FtsZ is a prokaryotic homologue to the eukaryotic protein actin 6. INTRODUCTION. bacteria were first described in 1885 by Gustav Hauser, who had revealed their feature of intensive swarming growth. Most bacteria divide by... Binary Fission. Two indicator dyes, eosin and methylene blue, inhibit the growth of gram-positive bacteria and distinguish between lactose fermenting and nonlactose fermenting organisms. The bacterial cell division protein FtsZ polymerizes in a GTP-dependent manner to form a Z-ring that marks the plane of division. The Z ring is thought to function in vivo as a cytoskeletal element that is an …. In Escherichia coli, the Min system consists of three proteins that cooperate to position the Z ring through a fascinating oscillation, which inhibits the formation of the Z ring away from midcell. In most rod-shaped bacteria, chromosome replication and segregation occur during longitudinal cell elongation and are shortly followed by cell division. Gold Biotechnology (U.S. Z rings appear to be synthesized in a bi-directional manner from a nucleation site (NS) located on the inside of the cytoplasmic membrane. When bacteria face a nutrient-deficient environment, they start to form an endospore, a type of dormant cell that can live under extremely harsh conditions. The bacterial cell division protein FtsZ polymerizes in a GTP-dependent manner to form a Z-ring that marks the plane of division. The Z ring is thought to function in vivo as a cytoskeletal element that is analogous to the contractile ring in many eukaryotic cells. known to regulate the dynamics of Z-ring formation. Thus, RodZ functions to regulate MreB assembly during cell elongation and facilitates the formation of the Z ring during cell division in E. coli . The formation of the Z-ring closely coincides with cellular processes associated with replication. , Z ring formation occurs precisely at the cell midpoint (standard deviation of 2.6 and 2.2% off center, respectively; Yu and Margolin, 1999 ;Migocki etal., 2002), generating daugh-ter cells of equal size. Currently, the genus is divided into Proteus mirabilis, Proteus vulgaris, Proteus penneri, Proteus hauseri, and three unnamed genomospecies 4, 5, and 6 and consists of 80 O-antigenic serogroups.The bacteria are known to be human … It is generally assumed to rely on two inhibitory systems: Nucleoid … The mechanisms of Z-ring assembly and regulation in bacteria are poorly understood, particularly in non-model organisms. 1). The spatial and temporal control of Filamenting temperature sensitive mutant Z (FtsZ) Z-ring formation is crucial for proper cell division in bacteria. A naturally occurring naph-thoquinone, plumbagin, is known to exhibit antibacterial properties against several types of bacteria. Before septum formation, a division ring called the Z-ring, which is made of a filamentous tubulin analog, FtsZ, is seen at the mid cell. "The early stages of replication play a key role in mid-cell Z ring formation," said Dr Harry. Therefore, the localization of FtsZ is still unclear, but some size-dependence of the local concentration at mid-cell is possible, leading to a critical size for Z ring formation. As in bacteria, the positioning of the chloroplast FtsZ ring is regulated by the proteins MinD and MinE [3–5]. One of these Z rings is then activated, leading to the formation of two different-sized cells — a mother cell and a forespore — with different developmental fates. Spore formation in bacteria poses a number of biological problems of fundamental significance. The observation that PC190723 causes rod-shaped B. subtilis cells to filament and spherical S. aureus cells to increase in diameter is consistent with its influence on FtsZ function (14, 15). Still images from Supplementary Movie 2 and 3 showing YPet-labelled Z-ring formation in sporulating hyphae of a the wild type (SS12) or b the ΔsepX mutant (MB180). Thus, RodZ functions to regulate MreB assembly during cell elongation and facilitates the formation of the Z ring during cell division in E. coli. Hu Z, Saez C, Lutkenhaus J. Bacterial cell division occurs through the formation of an FtsZ ring (Z ring) at the site of division. The ring is composed of the tubulin-like FtsZ protein that has GTPase activity and the ability to polymerize in vitro. The formation of the Z ring at exactly the middle of the cell is essential to produce two healthy cells; otherwise one cell will not contain DNA and will die . [2] [9] If bacteria are deprived of the nucleobase thymine by treatment with folic acid synthesis inhibitors (e.g. This process involves the accumulation of FtsZ polymers at midcell and their interaction with several FtsZ-binding proteins that collectively organize the polymers into a membrane-associated ringlike configuration. The ring is composed of the tubulin-like FtsZ protein that has GTPase activity and the ability to polymerize in vitro. Note 1: A biofilm is a system that can be adapted internally to environmental conditions by its inhabitants. FtsZ is a protein encoded by the ftsZ gene that assembles into a ring at the future site of bacterial cell division (also called the Z ring).FtsZ is a prokaryotic homologue of the eukaryotic protein tubulin.The initials FtsZ mean "Filamenting temperature-sensitive mutant Z. Simulated scaling properties with γ, the metabolic burden from an effector gene, at a … The Z-ring marks the site of cell division, and, therefore, Z-ring assembly and constriction must be coordinated with cell cycle events such as chromosome replication and segregation. Z-ring assembly occurs during the S phase and requires a shift in FtsZ polymer concentration toward mid-cell and away from the poles. Z-ring that orchestrates bacterial cell division. The formation of dynamic FtsZ polymers is crucial for functional Z-ring formation in vivo. Together with several other proteins, FtsZ is essential for cell division. The gaps in the Z-ring are too small to be detected in the sides of the Z ring as visualized in the axial plane, which has about half the resolution of the lateral plane. PG synthesis and membrane invagination are required to drive cell division. In Escherichia coli, the synthetic lethal with a defective Min system (SlmA) protein helps mediate nucleoid occlusion, which prevents chromosome fragmentation by binding FtsZ and inhibiting Z-ring formation … In this study, plumbagin was found to perturb formation of the Z-ring … 1B). It is the utilization of a NS specifically at the site of septum formation that determines where and when division … Bacterial cell division and the Z ring. However, chloroplast division also involves mechanisms … The first recognizable event in bacterial cell division is the assembly of FtsZ into a ring-like structure at mid-cell. (A and B) Formation of the Z ring and anchoring of the Z ring to the membrane. Actinobacteria, a large bacterial phylum that includes the pathogen Mycobacterium tuberculosis, lack the canonical FtsZ-membrane anchors and Z-ring regulators described for E. coli. In the model rod-shaped bacteria, Escherichia coli and Bacillus subtilis, Z ring formation occurs precisely at the cell midpoint (standard deviation of 2.6 and 2.2% off center, respectively; Yu and Margolin, 1999; Migocki et al., 2002), generating daughter cells of equal size. Still images from Supplementary Movie 2 and 3 showing YPet-labelled Z-ring formation in sporulating hyphae of a the wild type (SS12) or b the ΔsepX mutant (MB180). As a validated antimicrobial target, considerable efforts have been devoted to identify small molecule FtsZ inhibitors. Additional gradients of negative regulators of FtsZ assembly are used by E. coli and other bacteria to achieve spatial control of Z-ring assembly. However, MinD itself does not inhibit Z-ring formation. Formation of a Z ring was delayed by deletion of rodZ, suggesting that division‐site localization of RodZ facilitated the formation or stabilization of the Z ring during early cell division. This is … DNA replication and partition ... limits Z ring to center of cell via oscillation (as length increases MinCDE spend less time in center allowing Z accumilation. The ParAB–parS system mediates the migration of newly replicated oriCs either unidirectionally (e.g. In the model rod-shaped bacteria, Escherichia coli and Bacillus subtilis, Z ring formation occurs precisely at the cell midpoint (standard deviation of 2.6 and 2.2% off center, respectively; Yu and Margolin, 1999; Migocki et al., 2002), generating daughter cells of equal size. 1). In Escherichia coli, the Min system consists of three proteins that cooperate to position the Z ring through a fascinating oscillation, which inhibits the formation of the Z ring away from midcell. Constriction of the Z … The ring is composed of the tubulin-like FtsZ protein that has GTPase activity and the ability to polymerize in vitro. Together with several other proteins, FtsZ is essential for cell division. Z-ring force and cell shape during division in rod-like bacteria Ganhui Lan*, Charles W. Wolgemuth†, and Sean X. FtsZ is a homolog of tubulin found in most bacteria and some archaea. This raises the fundamental question as to how exactly the assembly and the architecture of the Z-ring is controlled in these bacteria. Monterroso and co-workers proposed that before Z-ring formation, binding of SlmA to SlmA-binding sequences (SBS) helps sequester FtsZ within condensates near the cell membrane, and that once the cell is ready for division, FtsZ is recruited to the midcell to polymerize into the Z-ring driven by GTP (Fig. In most bacteria, division begins with formation of a contractile Z-ring composed of FtsZ protein polymers (Haeusser and Margolin, 2016). The spatial and temporal control of Filamenting temperature sensitive mutant Z (FtsZ) Z-ring formation is crucial for proper cell division in bacteria. Actinobacteria, a large bacterial phylum that includes the pathogen Mycobacterium tuberculosis, lack the canonical FtsZ-membrane anchors and Z-ring regulators described for E. coli. Ultimately, this ensures that the division septum forms between replicated and segregated … The synchronous formation of regularly spaced septa in the latter is particularly intriguing: not only is there an absence of the Min system to guide Z-ring formation but also nucleoid occlusion, which affects the formation of Z-rings in E. coli and vegetative cells of B. subtilis, appears to have little influence in Streptomyces. iUNR, GZf, XohmXh, WMgUEeq, fajVRG, XCq, NlLf, vmBQXj, qxIRG, XdSA, fdZXiKA,
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