Since their discovery in the 20th century, antibiotics have been prescribed for patients with bacterial infections. The first commercially available antibiotic was penicillin, which was discovered in 1928 by Alexander Fleming in St. Marys Hospital, UK. Penicillin was effective to inhibit the growth of disease-causing microorganisms. However, in 1947, four years after the mass-production of penicillin, the first penicillin resistance case was identified. Since then, scientists have been looking for new targets to inhibit the bacterial growth. Among them, the bacterial cell division protein, filament temperature-sensitive Z (FtsZ), is a promising target for the development of new antibiotics. FtsZ protein is an essential protein in bacterial cytoplasmic division. A GTPase active site is formed when two FtsZ monomers are joined together in head-to-tail manner. The presence of GTP induces the polymerization of FtsZ in the middle of the cell. FtsZ polymers act as a platform to recruit other cell ...
FtsZ plays an important role in bacterial cell division by polymerizing to form the Z ring at the site of cytokinesis. Phytochemicals are known to disrupt bacterial cell division through inhibition of FtsZ assembly. In the present study phytochemicals like eugenol, trans-cinnamic acid, 4-formyl cinnamic acid, naringenin and caffeic acid were were tested for their potential to inhibit cell division. Effect of these antimicrobial compounds on the growth of E. coli was determined and the inhibition of FtsZ assembly in vitro was investigated. The present study revealed trans-cinnamic acid as the most potent inhibitor of FtsZ assembly ...
Suprastructures and dynamic properties of Mycobacterium tuberculosis FtsZ.s profile, publications, research topics, and co-authors
Global Markets Directs, Cell Division Protein FtsZ (ftsz) - Pipeline Review, H2 2016, provides in depth analysis on Cell Division Protein FtsZ (ftsz) targeted pipeline therapeutics. The
Microvilli at the apical surface of enterocytes allow the efficient absorption of nutrients in the intestine. Ezrin activation by its phosphorylation at T567 is important for microvilli development, but how ezrin phosphorylation is controlled is not well understood. We demonstrate that a subset of kinases that phosphorylate ezrin closely co-distributes with apical recycling endosome marker rab11a in the subapical domain. Expression of dominant-negative rab11a mutant or depletion of the rab11a-binding motor protein myosin Vb prevents the subapical enrichment of rab11a and these kinases and inhibits ezrin phosphorylation and microvilli development, without affecting the polarized distribution of ezrin itself. We observe a similar loss of the subapical enrichment of rab11a and the kinases and reduced phosphorylation of ezrin in Microvillus inclusion disease, which is associated with MYO5B mutations, intestinal microvilli atrophy and mal-absorption. Thus, part of the machinery for ezrin activation ...
Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity.
Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity.
The FtsZ protein forms a dynamic polymeric ring structure, which functions as the guiding scaffold for septal invagination at the mid-cell site during cytokinesis in bacterial cells (Bi & Lutkenhaus, 1991). FtsZ forms polymers in a GTP-dependent manner in vivo and under different cationic conditions in vitro (Andreu et al., 2002; Beuria et al., 2003;Bi & Lutkenhaus, 1991; Bramhill & Thompson, 1994; Caplan & Erickson, 2003; Diaz et al., 2001; Erickson et al., 1996; Lu et al., 1998; Mingorance et al., 2001; Mukherjee & Lutkenhaus, 1994, 1999; Rivas et al., 2000; Romberg et al., 2001; Scheffers et al., 2001; Wang et al., 1997; White et al., 2000; Yu & Margolin, 1997). The rate of polymerization of the FtsZ protein of Mycobacterium tuberculosis H37Rv (MtFtsZ) is remarkably slow when compared to that of the Escherichia coli FtsZ protein (EcFtsZ) (Bramhill & Thompson, 1994; Mukherjee & Lutkenhaus, 1999; White et al., 2000). While polymerization of EcFtsZ reaches steady state in 30 s after the addition ...
Highlights: • Palladin is involved in myogenesis in vitro. • Palladin knockdown by siRNA increases myoblast proliferation, viability and differentiation. • Palladin knockdown decreases C2C12 myoblast migration ability. - Abstract: The actin-associated protein palladin has been shown to be involved in differentiation processes in non-muscle tissues. However, but its function in skeletal muscle has rarely been studied. Palladin plays important roles in the regulation of diverse actin-related signaling in a number of cell types. Since intact actin-cytoskeletal remodeling is necessary for myogenesis, in the present study, we pursue to investigate the role of actin-associated palladin in skeletal muscle differentiation. Palladin in C2C12 myoblasts is knocked-down using specific small interfering RNA (siRNA). The results show that down-regulation of palladin decreased migratory activity of mouse skeletal muscle C2C12 myoblasts. Furthermore, the depletion of palladin enhances C2C12 vitality and ...
The earliest stage in bacterial cell division is the formation of a ring, composed of the tubulin-like protein FtsZ, at the division site. Tight spatial and temporal regulation of Z-ring formation is required to ensure that division occurs precisely at midcell between two replicated chromosomes. However, the mechanism of Z-ring formation and its regulation in vivo remain unresolved. Here we identify the defect of an interesting temperature-sensitive ftsZ mutant (ts1) of Bacillus subtilis. At the nonpermissive temperature, the mutant protein, FtsZ(Ts1), assembles into spiral-like structures between chromosomes. When shifted back down to the permissive temperature, functional Z rings form and division resumes. Our observations support a model in which Z-ring formation at the division site arises from reorganization of a long cytoskeletal spiral form of FtsZ and suggest that the FtsZ(Ts1) protein is captured as a shorter spiral-forming intermediate that is unable to complete this reorganization ...
Therapeutic irradiation can induce cognitive impairments without necessarily causing the gross histologic disruption classically associated with exposure to high radiation doses ( 1). Given that postmitotic neurons are generally considered to be relatively radioresistant, new approaches/techniques have been used to identify other "targets" that may ultimately contribute to the pathogenesis of radiation-induced cognitive injury. Data now exist regarding neurogenesis ( 14, 15), specific genetic factors ( 33) or receptor expression ( 34), and show that changes in these end points can be associated with subsequent cognitive impairments. Still, there is considerable uncertainty regarding how molecular and cellular events within specific neuronal populations are translated into changes that affect behavioral performance. Understanding such changes will be critical to the development of strategies or approaches necessary to prevent or treat the cognitive changes induced by therapeutic irradiation of ...
FtsZ has a GTPase activity that is associated with assembly and required for the dynamics of FtsZ polymers (24). In this study, we have investigated the properties of FtsZ2 that can support cell division despite having a dramatically reduced GTPase activity. We found that FtsZ2 is unable to assemble in vitro; however, it copolymerized upon addition of FtsZ, provided FtsZ is above the critical concentration. This supports a model for cooperative assembly of FtsZ polymers. Significantly, the stability of the copolymers increased with increasing FtsZ2 incorporation, implying FtsZ2 polymers, if formed, would be stable. Since FtsZ2 can support viability, our results suggest that stable FtsZ filaments are able to function in cell division. This result has important implications for the role of the Z ring in cell division, because it argues that constriction of the Z ring can occur through forces acting on FtsZ filaments.. FtsZ2 was isolated as an allele of ftsZ that was resistant to the cell division ...
In vivo characterization of Escherichia coli ftsZ mutants: effects on Z-ring structure and function.s profile, publications, research topics, and co-authors
In neurons certain mRNA transcripts are transported to synapses through mechanisms that are not fully understood. Here we report that the heterogeneous nuclear ribonucleoprotein CBF-A (CArG Box binding Factor A) facilitates dendritic transport and localization of activity-regulated cytoskeleton-associated protein (Arc), brain-derived neurotrophic factor (BDNF), and calmodulin-dependent protein kinase II (CaMKII alpha) mRNAs. We discovered that, in the adult mouse brain, CBF-A has a broad distribution. In the nucleus, CBF-A was found at active transcription sites and interchromosomal spaces and close to nuclear pores. In the cytoplasm, CBF-A localized to dendrites as well as pre- and postsynaptic sites. CBF-A was found in synaptosomal fractions, associated with Arc, BDNF, and CaMKII alpha mRNAs. Electrophoretic mobility shift assays demonstrated a direct interaction mediated via their hnRNP A2 response element (A2RE)/RNA trafficking sequence (RTS) elements located in the 3 untranslated regions. ...
Cooperativity in the structuring equilibria of FtsZ and Z-ring disassembly.The model that emerges out of the in vitro work led us to determine the amount of SulA required to inhibit Z-ring formation in vivo. SulA inhibited Z-ring formation in vivo with somewhat lower stoichiometry compared to what we observed in vitro. Quantitative immunoblotting revealed that MalE-SulA resulted in Z-ring disassembly when it reached ≤50% of the total cellular level of FtsZ. A previous study likewise found that a reduction in FtsZ levels by as little as 30 to 40% was sufficient to block cell division in E. coli (15). Why do Z rings disappear when the level of FtsZ decreases by only 30 to 50%?. It has been estimated that 30% of cellular FtsZ in E. coli is actually present in the Z ring (2). The estimates for intracellular concentration of FtsZ vary between strains but are generally 6 to 7 μM as we determined here (38, 61). This means that 2 μM of FtsZ is present in the ring with another 0.9 μM free in the ...
Cell division in bacteria is a highly controlled and regulated process. FtsZ, a bacterial cytoskeletal protein, forms a ring-like structure known as the Z-ring and recruits more than a dozen other cell division proteins. The Min system oscillates between the poles and inhibits the Z-ring formation at the poles by perturbing FtsZ assembly. This leads to an increase in the FtsZ concentration at the mid-cell and helps in Z-ring positioning. MinC, the effector protein, interferes with Z-ring formation through two different mechanisms mediated by its two domains with the help of MinD. However, the mechanism by which MinD triggers MinC activity is not yet known. We showed that MinD directly interacts with FtsZ with an affinity stronger than the reported MinC-FtsZ interaction. We determined the MinD-binding site of FtsZ using computational, mutational and biochemical analyses. Our study showed that MinD binds to the H10 helix of FtsZ. Single-point mutations at the charged residues in the H10 helix ...
Cell division in bacteria is facilitated by a polymeric ring structure, the Z ring, composed of tubulin-like FtsZ protofilaments. Recently it has been shown that in Bacillus subtilis, the Z ring forms through the cell cycle-mediated remodelling of a helical FtsZ polymer. To investigate how this occurs in vivo, we have exploited a unique temperature-sensitive strain of B. subtilis expressing the mutant protein FtsZ(Ts1). FtsZ(Ts1) is unable to complete Z ring assembly at 49°C, becoming trapped at an intermediate stage in the helix-to-ring progression. To determine why this is the case, we used a combination of methods to identify the specific defect of the FtsZ(Ts1) protein in vivo. Our results indicate that while FtsZ(Ts1) is able to polymerize normally into protofilaments, it is defective in the ability to support lateral associations between these filaments at high temperatures. This strongly suggests that lateral FtsZ association plays a crucial role in the polymer transitions that lead to ...
Distribution of ezrin expression in primary and recurrent tumours. Bar charts visualizing the distribution of mean A) cytoplasmic and B) membranous ezrin expres
The high-resolution visualization of FtsZ polymerization and depolymerization on a lipid membrane allowed us to directly observe its assembly/disassembly characteristics and its spatial regulation by the Min proteins. In particular, we could assemble dynamic FtsZ filament bundles that anneal and branch, resulting in a dynamic network on supported bilayers. By using a minus end-capping fragment, NZ, we can show that the protofilament ends are generated, and the proteins may be exchanged, constantly throughout the length of the filament bundles. This specific dynamic turnover, quite distinct from the dynamics observed in microtubules, constitutes the basis for Z-ring positioning by the Min protein machinery.. The Z-ring presumably consists laterally of 6-10 protofilaments (7, 21, 49, 50). FtsZ first polymerizes into single-stranded short protofilaments and subsequently interacts laterally and longitudinally to settle into longer, staggered bundles. The exchange of subunits is occurring not only ...
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Sample immunohistochemical images. Images representing A) a primary tumour with strong membranous and moderate cytoplasmic ezrin expression in nearly 100% of ce
FtsZ is a widely conserved tubulin-like GTPase that directs bacterial cell division. This protein assembly machine works cooperatively polymerizing into single-stranded filaments, by means of self-switching between inactive and actively associating monomer conformations ...
Monoclonal Antibody for studying ezrin (Thr567) phosphate/moesin (Thr558) phosphate/radixin (Thr564) phosphate in the Cytoskeletal Signaling research area.
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TY - JOUR. T1 - Ezrin/radixin/moesin proteins differentially regulate endothelial hyperpermeability after thrombin. AU - Adyshev, Djanybek M.. AU - Dudek, Steven M.. AU - Moldobaeva, Nurgul. AU - Kim, Kyung mi. AU - Ma, Shwu Fan. AU - Kasa, Anita. AU - Garcia, Joe G.N.. AU - Verin, Alexander Dmitriyevich. PY - 2013/8/1. Y1 - 2013/8/1. N2 - Endothelial cell (EC) barrier disruption induced by inflammatory agonists such as thrombin leads to potentially lethal physiological dysfunction such as alveolar flooding, hypoxemia, and pulmonary edema. Thrombin stimulates paracellular gap and F-actin stress fiber formation, triggers actomyosin contraction, and alters EC permeability through multiple mechanisms that include protein kinase C (PKC) activation. We previously have shown that the ezrin, radixin, and moesin (ERM) actin-binding proteins differentially participate in sphingosine-1 phosphate-induced EC barrier enhancement. Phosphorylation of a conserved threonine residue in the COOH-terminus of ERM ...
Bacterial cell division is restricted to the middle of the cell. This, say Kyoko Suefuji, Regina Valluzzi, and Debabrata RayChaudhuri (Tufts University, Boston, MA), can be explained by polymerization events that oscillate between the two ends of the cell.. The polymerization process forms filaments of MinD at one end of the cell, which sequester MinC from the middle of the cell, thus leaving the bacterial cell division protein FtsZ to do its job. An additional component, MinE, forms a cap on the MinCD crescent so that the inhibitor, MinC, cannot reach the central FtsZ.. These proteins must inhibit division at both ends, and they do so by oscillating from one end of the cell to the other every 50 seconds. In several existing models, self-assembly is a key part of this oscillation. Joe Lutkenhaus (University of Kansas, Kansas City, KS) has recently seen self-assembly of MinD on lipid vesicles, with diffraction patterns suggesting a regular structure.. But the Tufts team is the first to visualize ...
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Cell division in Chlamydiae is poorly understood as apparent homologs to most conserved bacterial cell division proteins are lacking and presence of elongation (rod shape) associated proteins indicate non-canonical mechanisms may be employed. The rod-shape determining protein MreB has been proposed as playing a unique role in chlamydial cell division. In other organisms, MreB is part of an elongation complex that requires RodZ for proper function. A recent study reported that the protein encoded by ORF CT009 interacts with MreB despite low sequence similarity to RodZ. The studies in this paper expand on those observations through protein structure, mutagenesis and cellular localization analyses. Structural analysis indicated that CT009 shares high level of structural similarity to RodZ, revealing the conserved orientation of two residues critical for MreB interaction. Substitutions eliminated MreB protein interaction and partial complementation provided by CT009 in RodZ deficient Escherichia ...
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The major cause of death in pancreatic cancer is due to metastases; therefore, it is important to study the mechanism by which the pancreatic cancer cells migrate and invade. This would help advance therapeutics and ultimately help prolong survival. Adenylyl cyclase-associated protein 1 (CAP1) is a scaffold protein that is involved in the regulation of actin microfilament formation, which ultimately leads to cell migration and invasion. CAP1 binds to G-actin inhibiting polymerization. We first tested whether CAP1 binds to adenylyl cyclase (AC) by performing co-immunoprecipitation. We found that CAP1 not only interacts with G-actin, but also with a number of AC isoforms: AC1, AC3, AC4 and AC7. Further studies need to be done to determine how CAP1/AC/G-actin interact and the impact of these interactions on the invasive behavior of pancreatic cancer cells ...
NMR structural characterization of the N-terminal domain of the adenylyl cyclase-associated protein (CAP) from Dictyostelium discoideum. Related
Rabbit polyclonal Ezrin / Radixin / Moesin antibody validated for WB, ELISA, IHC and tested in Human and Mouse. Immunogen corresponding to synthetic peptide
Bacterial cell division occurs by a highly conserved process predominantly, termed binary fission, that requires the microbial homologue of tubulin, FtsZ. of VX-765 manufacture the unipolar development and FtsZ-independent fission of this coccoid patient. This system of cell department offers not really been recorded in additional human being microbial pathogens recommending the potential for developing is definitely the leading microbial trigger of sexually sent attacks. will not really communicate FtsZ, which is definitely required for the extremely conserved procedure of binary fission that most bacterias use to separate. non-etheless, it provides been believed that this microbial virus splits by binary fission. We Rabbit Polyclonal to Cox1 present right here that splits VX-765 manufacture by a polarized cell department procedure that can be identical to the flourishing procedure of some various other bacterias that absence FtsZ, such as the Planctomycetes. This story setting of cell ...
In most bacteria and archaea, filaments of FtsZ protein organize cell division. FtsZ forms a ring structure at the division site and starts the recruitment of 10 to 20 downstream proteins that together form a multiprotein complex termed the divisome. The divisome is thought to facilitate many of the steps required to make two cells out of one. FtsQ and FtsB are part of the divisome, with FtsQ being a central hub, interacting with most... ...
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In the present study, our comprehensive behavioral test battery revealed that Apc1638T/1638T mice shows impaired learning and memory, increased locomotor activity, mildly increased depression-like behavior, reduced anxiety-like behavior and mildly decreased social interaction behavior. In the hippocampal CA1 region of Apc1638T/1638T mice, the dendritic spine density and size are reduced, the PSD was smaller, and LTP was impaired. Taken together, our findings provide the first direct evidence of neuropsychological roles for the C-terminus of Apc tumor suppressor.. Apc1638T/1638T mice showed hyperactivity, impaired memory, increased depression-like behavior, and decreased social interaction. These behavioral characteristics are often linked to symptoms of schizophrenia (see Supplementary Table 11 in [15]) and observed in many animal models of schizophrenia [15-19]. In particular, Apc1638T/1638T mice showed a marked deficit in the performance of the working memory task. Impaired working memory is ...
Endocytosis of Trk (tropomyosin-related kinase) receptors is critical for neurotrophin signal transduction and biological functions. However, the mechanism governing endocytosis of TrkB (tropomyosin-related kinase B) and the specific contributions of TrkB endocytosis to downstream signaling are unknown. In this study, we report that blocking clathrin, dynamin, or AP2 in cultured neurons of the central nervous system inhibited brain-derived neurotrophic factor (BDNF)-induced activation of Akt but not ERK. Treating neurons with the clathrin inhibitor monodansylcadaverine or a peptide that blocks dynamin function specifically abrogated Akt pathway activation in response to BDNF but did not affect the response of other downstream effectors or the up-regulation of immediate early genes neuropeptide Y and activity-regulated cytoskeleton-associated protein. Similar effects were found in neurons expressing small interfering RNA to silence AP2 or a dominant negative form of dynamin that inhibits ...
Cell division in the Gram-positive bacterium Streptomyces coelicolor starts with the assembly of the tubulin homologue FtsZ into a cytokinetic ring (the Z ring) at the site of septation. In stark contrast to the binary fission of most bacteria, the syncytial hyphal cells of S. coelicolor exploit two types of cell division with strikingly different outcomes depending on the developmental stage. The main goal of this study has been to identify developmental mechanisms that modulate this differential performance of the basic cell division machinery.. By isolation and characterization of a non-sporulating ftsZ mutant, we demonstrated that the requirements for Z-ring formation differ between the two types of septation. The ftsZ17(Spo) mutation abolished septation without overtly affecting vegetative growth. This mutant was defective in the assembly of FtsZ into regularly spaced Z rings in sporogenic hyphae, suggesting that the assembly of Z rings is developmentally controlled during ...
ASC is an adaptor protein which contains two protein-protein interaction domains; N-terminal - pyrin domain (PYC) and C-terminal - caspase recruitment domain (CARD).. ASC plays an important role in inflammation and apoptosis. It is a component of several inflammatory complexes, inflammasomes, which are important for caspase-1 activation, processing and secretion of pro-inflammatory cytokines (IL-1β, IL-18). It promotes pyropoptosis in macrophages and induces caspase-mediated apoptosis (involving caspase-8 and caspase-9).. Additionally, ASC is involved in transcriptional control of cytokine and chemokine expression independent of the inflammasome.. ...
Background: Inflammatory responses play a key role in the pathophysiology of myocardial ischemia-reperfusion (I/R) injury. ASC is an adaptor protein that forms inflammasome whose activation leads to caspase-1-dependent interleukin (IL)-1β generation and subsequent inflammatory responses; however, the role of ASC in myocardial I/R injury remains to be determined.. Methods and Results: ASC deficient (ASC−/−) and wild-type (WT) mice were subjected to 30 min LAD occlusion, followed by reperfusion. ASC−/− mice showed improved LV dysfunction (%FS: 34.0% vs. 25.7% at 14 days p,0.01), reduced infarct area/area at risk (IA/AAR: 18.7% vs. 28.6% at 48 h, p,0.01), and scar formation (scar/LV area: 9.7% vs. 14.6% at 14 days, p,0.01) after myocardial I/R. Immunostaining revealed decreased infiltration of macrophages (Mac3) and neutrophils (Gr-1), but not neovascularization (CD31), in the injured myocardium of the ASC−/− mice. Real-time RT-PCR and ELISA analyses demonstrated that the myocardial ...
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The ERM protein family consists of three closely related proteins, ezrin, radixin and moesin. The three paralogs, ezrin, radixin and moesin, are present in vertebrates, whereas other species have only one ERM gene. Therefore, in vertebrates these paralogs likely arose by gene duplication. ERM proteins are highly conserved throughout evolution. More than 75% identity is observed in the N-terminal and the C-terminal of vertebrates (ezrin, radixin, moesin), Drosophila (dmoesin) and C. elegans (ERM-1) homologs. ERM molecules contain the following three domains: N-terminal globular domain, also called FERM domain (Band 4.1, ezrin, radixin, moesin). The FERM domain allows ERM proteins to interact with integral proteins of the plasma membrane, or scaffolding proteins localized beneath the plasma membrane. The FERM domain is composed of three subdomains (F1, F2, F3) that are arranged as a cloverleaf. extended alpha-helical domain. charged C-terminal domain. This domain mediates the interaction with ...