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Journal articles on the topic 'FTSAQ'

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Published: 5 June 2025

Last updated: 1 August 2025

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1

Goehring, Nathan W., Ivana Petrovska, Dana Boyd, and Jon Beckwith. "Mutants, Suppressors, and Wrinkled Colonies: Mutant Alleles of the Cell Division Gene ftsQ Point to Functional Domains in FtsQ and a Role for Domain 1C of FtsA in Divisome Assembly." Journal of Bacteriology 189, no. 2 (2006): 633–45. http://dx.doi.org/10.1128/jb.00991-06.

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ABSTRACT Cell division in Escherichia coli requires the concerted action of at least 10 essential proteins. One of these proteins, FtsQ, is physically associated with multiple essential division proteins, including FtsK, FtsL, FtsB, FtsW, and FtsI. In this work we performed a genetic analysis of the ftsQ gene. Our studies identified C-terminal residues essential for FtsQ's interaction with two downstream proteins, FtsL and FtsB. Here we also describe a novel screen for cell division mutants based on a wrinkled-colony morphology, which yielded several new point mutations in ftsQ. Two of these m

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Hale, Cynthia A., and Piet A. J. de Boer. "ZipA Is Required for Recruitment of FtsK, FtsQ, FtsL, and FtsN to the Septal Ring in Escherichia coli." Journal of Bacteriology 184, no. 9 (2002): 2552–56. http://dx.doi.org/10.1128/jb.184.9.2552-2556.2002.

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ABSTRACT The septal ring in Escherichia coli consists of at least nine essential gene products whose order of assembly resembles a mostly linear dependency pathway: FtsA and ZipA directly bind FtsZ polymers at the prospective division site, followed by the sequential addition of FtsK, FtsQ, FtsL, FtsW, FtsI, and FtsN. Recruitment of FtsK and all downstream components requires the prior localization of FtsA. Here we show that recruitment of FtsK, FtsQ, FtsL, and FtsN equally requires ZipA. The results imply that association of both FtsA and ZipA with FtsZ polymers is needed for further maturati

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3

Chen, Joseph C., David S. Weiss, Jean-Marc Ghigo, and Jon Beckwith. "Septal Localization of FtsQ, an Essential Cell Division Protein in Escherichia coli." Journal of Bacteriology 181, no. 2 (1999): 521–30. http://dx.doi.org/10.1128/jb.181.2.521-530.1999.

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ABSTRACT Septation in Escherichia coli requires several gene products. One of these, FtsQ, is a simple bitopic membrane protein with a short cytoplasmic N terminus, a membrane-spanning segment, and a periplasmic domain. We have constructed a merodiploid strain that expresses both FtsQ and the fusion protein green fluorescent protein (GFP)-FtsQ from single-copy chromosomal genes. The gfp-ftsQgene complements a null mutation in ftsQ. Fluorescence microscopy revealed that GFP-FtsQ localizes to the division site. Replacing the cytoplasmic and transmembrane domains of FtsQ with alternative membrane

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Eberhardt, Christian, Lars Kuerschner та David S. Weiss. "Probing the Catalytic Activity of a Cell Division-Specific Transpeptidase In Vivo with β-Lactams". Journal of Bacteriology 185, № 13 (2003): 3726–34. http://dx.doi.org/10.1128/jb.185.13.3726-3734.2003.

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ABSTRACT Penicillin-binding protein 3 (PBP3; also called FtsI) is a transpeptidase that catalyzes cross-linking of the peptidoglycan cell wall in the division septum of Escherichia coli. To determine whether the catalytic activity of PBP3 is activated during division, we assayed acylation of PBP3 with three β-lactams (cephalexin, aztreonam, and piperacillin) in growing cells. Acylation of PBP3 with cephalexin, but not aztreonam or piperacillin, appeared to be stimulated by cell division. Specifically, cephalexin acylated PBP3 about 50% faster in a population of dividing cells than in a populat

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5

Park, Kyung-Tae, Sebastien Pichoff, Shishen Du, and Joe Lutkenhaus. "FtsA acts through FtsW to promote cell wall synthesis during cell division in Escherichia coli." Proceedings of the National Academy of Sciences 118, no. 35 (2021): e2107210118. http://dx.doi.org/10.1073/pnas.2107210118.

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In Escherichia coli, FtsQLB is required to recruit the essential septal peptidoglycan (sPG) synthase FtsWI to FtsA, which tethers FtsZ filaments to the membrane. The arrival of FtsN switches FtsQLB in the periplasm and FtsA in the cytoplasm from a recruitment role to active forms that synergize to activate FtsWI. Genetic evidence indicates that the active form of FtsQLB has an altered conformation with an exposed domain of FtsL that acts on FtsI to activate FtsW. However, how FtsA contributes to the activation of FtsW is not clear, as it could promote the conformational change in FtsQLB or act

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6

NURZHAN, SHILMURZAYEV, TURSYNBAYEV ABYLAY, CHANDAN PAL SINGH, AN IGOR, and OMIRKUL BAISEYIT. "DEVELOPMENT OF ANALYSIS AND EVALUATION SKILLS IN A PHYSICS TEACHING THROUGH PRACTICAL WORK." International Journal Of Multidisciplinary Research And Studies 05, no. 06 (2022): 01–15. http://dx.doi.org/10.33826/ijmras/v05i06.3.

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This research paper addresses how to enhance analysis and evaluation skills in physics lessons using practical or lab work. Analysis and evaluation skills are very important for high school science students that can lead to developing critical thinking also, especially where English is a third-level language. Practicality plays a very important role in understanding complex and confusing topics, so integrating physics lessons with teaching practical work can improve a significant level of understanding. We have researched and analyzed data after applying for practical work in regular lessons a

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Dr., SHILMURZAYEV NURZHAN, TURSYNBAYEV ABYLAY Dr., CHANDAN PAL SINGH Dr., AN IGOR Dr., and OMIRKUL BAISEYIT5 Dr. "DEVELOPMENT OF ANALYSIS AND EVALUATION SKILLS IN A PHYSICS TEACHING THROUGH PRACTICAL WORK." International Journal Of Multidisciplinary Research And Studies 05, no. 06 (2022): 19–33. https://doi.org/10.33826/ijmras/v05i06.3.

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This research paper addresses how to enhance analysis and evaluation skills in physics lessons using practical or lab work. Analysis and evaluation skills are very important for high school science students that can lead to developing critical thinking also, especially where English is a third-level language. Practicality plays a very important role in understanding complex and confusing topics, so integrating physics lessons with teaching practical work can improve a significant level of understanding. We have researched and analyzed data after applying for practical work in regular lessons a

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8

Vinella, Daniel, Michael Cashel, and Richard D’Ari. "Selected Amplification of the Cell Division Genes ftsQ-ftsA-ftsZ in Escherichia coli." Genetics 156, no. 4 (2000): 1483–92. http://dx.doi.org/10.1093/genetics/156.4.1483.

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Abstract Rapidly growing Escherichia coli is unable to divide in the presence of the antibiotic mecillinam, whose direct target is penicillin-binding protein 2 (PBP2), responsible for the elongation of the cylindrical portion of the cell wall. Division can be restored in the absence of PBP2 activity by increasing the concentration of the cell division proteins FtsQ, FtsA, and FtsZ. We tried to identify regulators of the ftsQ-ftsA-ftsZ operon among mecillinam-resistant mutants, which include strains overexpressing these genes. By insertional mutagenesis with mini-Tn10 elements, we selected for

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Marbouty, Martial, Khalil Mazouni, Cyril Saguez, Corinne Cassier-Chauvat, and Franck Chauvat. "Characterization of the Synechocystis Strain PCC 6803 Penicillin-Binding Proteins and Cytokinetic Proteins FtsQ and FtsW and Their Network of Interactions with ZipN." Journal of Bacteriology 191, no. 16 (2009): 5123–33. http://dx.doi.org/10.1128/jb.00620-09.

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ABSTRACT Because very little is known about cell division in noncylindrical bacteria and cyanobacteria, we investigated 10 putative cytokinetic proteins in the unicellular spherical cyanobacterium Synechocystis strain PCC 6803. Concerning the eight penicillin-binding proteins (PBPs), which define three classes, we found that Synechocystis can survive in the absence of one but not two PBPs of either class A or class C, whereas the unique class B PBP (also termed FtsI) is indispensable. Furthermore, we showed that all three classes of PBPs are required for normal cell size. Similarly, the putati

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Reddy, Manjula. "Role of FtsEX in Cell Division of Escherichia coli: Viability of ftsEX Mutants Is Dependent on Functional SufI or High Osmotic Strength." Journal of Bacteriology 189, no. 1 (2006): 98–108. http://dx.doi.org/10.1128/jb.01347-06.

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ABSTRACT In Escherichia coli, at least 12 proteins, FtsZ, ZipA, FtsA, FtsE/X, FtsK, FtsQ, FtsL, FtsB, FtsW, FtsI, FtsN, and AmiC, are known to localize to the septal ring in an interdependent and sequential pathway to coordinate the septum formation at the midcell. The FtsEX complex is the latest recruit of this pathway, and unlike other division proteins, it is shown to be essential only on low-salt media. In this study, it is shown that ftsEX null mutations are not only salt remedial but also osmoremedial, which suggests that FtsEX may not be involved in salt transport as previously thought.

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11

Yi, Qing-Ming, Susan Rockenbach, John E. Ward, and Joe Lutkenhaus. "Structure and expression of the cell division genes ftsQ, ftsA and ftsZ." Journal of Molecular Biology 184, no. 3 (1985): 399–412. http://dx.doi.org/10.1016/0022-2836(85)90290-6.

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12

Goehring, Nathan W., Carine Robichon, and Jon Beckwith. "Role for the Nonessential N Terminus of FtsN in Divisome Assembly." Journal of Bacteriology 189, no. 2 (2006): 646–49. http://dx.doi.org/10.1128/jb.00992-06.

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ABSTRACT FtsN, the last essential protein in the cell division localization hierarchy in Escherichia coli, has several peculiar characteristics, suggesting that it has a unique role in the division process despite the fact that it is conserved in only a subset of bacteria. In addition to suppressing temperature-sensitive mutations in ftsA, ftsK, ftsQ, and ftsI, overexpression of FtsN can compensate for a complete lack of FtsK in the cell. We examined the requirements for this phenomenon. We found that the N-terminal terminal region (cytoplasmic and transmembrane domains) is critical for suppre

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Martin, Miriam E., Michael J. Trimble, and Yves V. Brun. "Cell cycle-dependent abundance, stability and localization of FtsA and FtsQ in Caulobacter crescentus." Molecular Microbiology 54, no. 1 (2004): 60–74. http://dx.doi.org/10.1111/j.1365-2958.2004.04251.x.

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14

Schmidt, Kari L., Nicholas D. Peterson, Ryan J. Kustusch, et al. "A Predicted ABC Transporter, FtsEX, Is Needed for Cell Division in Escherichia coli." Journal of Bacteriology 186, no. 3 (2004): 785–93. http://dx.doi.org/10.1128/jb.186.3.785-793.2004.

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ABSTRACT FtsE and FtsX have homology to the ABC transporter superfamily of proteins and appear to be widely conserved among bacteria. Early work implicated FtsEX in cell division in Escherichia coli, but this was subsequently challenged, in part because the division defects in ftsEX mutants are often salt remedial. Strain RG60 has an ftsE::kan null mutation that is polar onto ftsX. RG60 is mildly filamentous when grown in standard Luria-Bertani medium (LB), which contains 1% NaCl, but upon shift to LB with no NaCl growth and division stop. We found that FtsN localizes to potential division sit

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Di Lallo, G., M. Fagioli, D. Barionovi, P. Ghelardini, and L. Paolozzi. "Use of a two-hybrid assay to study the assembly of a complex multicomponent protein machinery: bacterial septosome differentiation." Microbiology 149, no. 12 (2003): 3353–59. http://dx.doi.org/10.1099/mic.0.26580-0.

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The ability of each of the nine Escherichia coli division proteins (FtsZ, FtsA, ZipA, FtsK, FtsQ, FtsL, FtsW, FtsI, FtsN) to interact with itself and with each of the remaining eight proteins was studied in 43 possible combinations of protein pairs by the two-hybrid system previously developed by the authors' group. Once the presumed interactions between the division proteins were determined, a model showing their temporal sequence of assembly was developed. This model agrees with that developed by other authors, based on the co-localization sequence in the septum of the division proteins fuse

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Mercer, Keri L. N., and David S. Weiss. "The Escherichia coli Cell Division Protein FtsW Is Required To Recruit Its Cognate Transpeptidase, FtsI (PBP3), to the Division Site." Journal of Bacteriology 184, no. 4 (2002): 904–12. http://dx.doi.org/10.1128/jb.184.4.904-912.2002.

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ABSTRACT The bacterial cell division protein FtsW has been suggested to perform two functions: stabilize the FtsZ cytokinetic ring, and facilitate septal peptidoglycan synthesis by the transpeptidase FtsI (penicillin-binding protein 3). We show here that depleting Escherichia coli cells of FtsW had little effect on the abundance of FtsZ rings but abrogated recruitment of FtsI to potential division sites. Analysis of FtsW localization confirmed and extended these results; septal localization of FtsW required FtsZ, FtsA, FtsQ, and FtsL but not FtsI. Thus, FtsW is a late recruit to the division s

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Descoteaux, A., and G. R. Drapeau. "Regulation of cell division in Escherichia coli K-12: probable interactions among proteins FtsQ, FtsA, and FtsZ." Journal of Bacteriology 169, no. 5 (1987): 1938–42. http://dx.doi.org/10.1128/jb.169.5.1938-1942.1987.

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18

Yeung, Leo W. Y., and Scott A. Mabury. "Are humans exposed to increasing amounts of unidentified organofluorine?" Environmental Chemistry 13, no. 1 (2016): 102. http://dx.doi.org/10.1071/en15041.

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Environmental context Polyfluorinated substances are anthropogenic chemicals that have been widely used in several industrial and commercial applications. Analysis of human plasma samples collected from Münster in Germany revealed, since the year 2000, increasing amounts and proportion of unidentified organofluorines. The increasing trend of unidentified organofluorines in plasma samples suggests that humans are being exposed to new and unidentified fluorinated products. Abstract Samples of human plasma (n=122) from two German cities (collected in 1982–2009, excluding 1994) and whole blood (n=

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Weiss, David S., Joseph C. Chen, Jean-Marc Ghigo, Dana Boyd, and Jon Beckwith. "Localization of FtsI (PBP3) to the Septal Ring Requires Its Membrane Anchor, the Z Ring, FtsA, FtsQ, and FtsL." Journal of Bacteriology 181, no. 2 (1999): 508–20. http://dx.doi.org/10.1128/jb.181.2.508-520.1999.

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ABSTRACT Assembly of the division septum in bacteria is mediated by several proteins that localize to the division site. One of these, FtsI (also called penicillin-binding protein 3) of Escherichia coli, consists of a short cytoplasmic domain, a single membrane-spanning segment, and a large periplasmic domain that encodes a transpeptidase activity involved in synthesis of septal peptidoglycan. We have constructed a merodiploid strain with a wild-type copy offtsI at the normal chromosomal locus and a genetic fusion of ftsI to the green fluorescent protein (gfp) at the lambda attachment site. gf

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Thakur, Payal, Vinoj Gopalakrishnan, Priya Saxena, et al. "Influence of Copper on Oleidesulfovibrio alaskensis G20 Biofilm Formation." Microorganisms 12, no. 9 (2024): 1747. http://dx.doi.org/10.3390/microorganisms12091747.

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Copper is known to have toxic effects on bacterial growth. This study aimed to determine the influence of copper ions on Oleidesulfovibrio alaskensis G20 biofilm formation in a lactate-C medium supplemented with variable copper ion concentrations. OA G20, when grown in media supplemented with high copper ion concentrations of 5, 15, and 30 µM, exhibited inhibited growth in its planktonic state. Conversely, under similar copper concentrations, OA G20 demonstrated enhanced biofilm formation on glass coupons. Microscopic studies revealed that biofilms exposed to copper stress demonstrated a chang

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Buddelmeijer, Nienke, Mirjam E. G. Aarsman, Arend H. J. Kolk, Miguel Vicente, and Nanne Nanninga. "Localization of Cell Division Protein FtsQ by Immunofluorescence Microscopy in Dividing and Nondividing Cells ofEscherichia coli." Journal of Bacteriology 180, no. 23 (1998): 6107–16. http://dx.doi.org/10.1128/jb.180.23.6107-6116.1998.

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ABSTRACT The localization of cell division protein FtsQ in Escherichia coli wild-type cells was studied by immunofluorescence microscopy with specific monoclonal antibodies. FtsQ could be localized to the division site in constricting cells. FtsQ could also localize to the division site in ftsQ1(Ts) cells grown at the permissive temperature. A hybrid protein in which the cytoplasmic domain and the transmembrane domain were derived from the γ form of penicillin-binding protein 1B and the periplasmic domain was derived from FtsQ was also able to localize to the division site. This result indicat

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Scheffers, Dirk-Jan, Carine Robichon, Gert Jan Haan, et al. "Contribution of the FtsQ Transmembrane Segment to Localization to the Cell Division Site." Journal of Bacteriology 189, no. 20 (2007): 7273–80. http://dx.doi.org/10.1128/jb.00723-07.

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ABSTRACT The Escherichia coli cell division protein FtsQ is a central component of the divisome. FtsQ is a bitopic membrane protein with a large C-terminal periplasmic domain. In this work we investigated the role of the transmembrane segment (TMS) that anchors FtsQ in the cytoplasmic membrane. A set of TMS mutants was made and analyzed for the ability to complement an ftsQ mutant. Study of the various steps involved in FtsQ biogenesis revealed that one mutant (L29/32R;V38P) failed to functionally insert into the membrane, whereas another mutant (L29/32R) was correctly assembled and interacted

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Corbin, Brian D., Brett Geissler, Mahalakshmi Sadasivam, and William Margolin. "Z-Ring-Independent Interaction between a Subdomain of FtsA and Late Septation Proteins as Revealed by a Polar Recruitment Assay." Journal of Bacteriology 186, no. 22 (2004): 7736–44. http://dx.doi.org/10.1128/jb.186.22.7736-7744.2004.

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ABSTRACT FtsA, a member of the ATPase superfamily that includes actin and bacterial actin homologs, is essential for cell division of Escherichia coli and is recruited to the Z ring. In turn, recruitment of later essential division proteins to the Z ring is dependent on FtsA. In a polar recruitment assay, we found that FtsA can recruit at least two late proteins, FtsI and FtsN, to the cell poles independently of Z rings. Moreover, a unique structural domain of FtsA, subdomain 1c, which is divergent in the other ATPase superfamily members, is sufficient for this recruitment but not required for

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Trespidi, Gabriele, Viola Camilla Scoffone, Giulia Barbieri, Giovanna Riccardi, Edda De Rossi, and Silvia Buroni. "Molecular Characterization of the Burkholderia cenocepacia dcw Operon and FtsZ Interactors as New Targets for Novel Antimicrobial Design." Antibiotics 9, no. 12 (2020): 841. http://dx.doi.org/10.3390/antibiotics9120841.

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The worldwide spread of antimicrobial resistance highlights the need of new druggable cellular targets. The increasing knowledge of bacterial cell division suggested the potentiality of this pathway as a pool of alternative drug targets, mainly based on the essentiality of these proteins, as well as on the divergence from their eukaryotic counterparts. People suffering from cystic fibrosis are particularly challenged by the lack of antibiotic alternatives. Among the opportunistic pathogens that colonize the lungs of these patients, Burkholderia cenocepacia is a well-known multi-drug resistant

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Karimova, Gouzel, Carine Robichon, and Daniel Ladant. "Characterization of YmgF, a 72-Residue Inner Membrane Protein That Associates with the Escherichia coli Cell Division Machinery." Journal of Bacteriology 191, no. 1 (2008): 333–46. http://dx.doi.org/10.1128/jb.00331-08.

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ABSTRACT Formation of the Escherichia coli division septum is catalyzed by a number of essential proteins (named Fts) that assemble into a ring-like structure at the future division site. Many of these Fts proteins are intrinsic transmembrane proteins whose functions are largely unknown. In the present study, we attempted to identify a novel putative component(s) of the E. coli cell division machinery by searching for proteins that could interact with known Fts proteins. To do that, we used a bacterial two-hybrid system based on interaction-mediated reconstitution of a cyclic AMP (cAMP) signal

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Uehara, Tsuyoshi, та James T. Park. "Role of the Murein Precursor UDP-N-Acetylmuramyl-l-Ala-γ-d-Glu- meso-Diaminopimelic Acid-d-Ala-d-Ala in Repression of β-Lactamase Induction in Cell Division Mutants". Journal of Bacteriology 184, № 15 (2002): 4233–39. http://dx.doi.org/10.1128/jb.184.15.4233-4239.2002.

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ABSTRACT Certain β-lactam antibiotics induce the chromosomal ampC β-lactamase of many gram-negative bacteria. The natural inducer, though not yet unequivocally identified, is a cell wall breakdown product which enters the cell via the AmpG permease component of the murein recycling pathway. Surprisingly, it has been reported that β-lactamase is not induced by cefoxitin in the absence of FtsZ, which is required for cell division, or in the absence of penicillin-binding protein 2 (PBP2), which is required for cell elongation. Since these results remain unexplained, we examined an ftsZ mutant and

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Du, Shishen, Sebastien Pichoff, and Joe Lutkenhaus. "FtsEX acts on FtsA to regulate divisome assembly and activity." Proceedings of the National Academy of Sciences 113, no. 34 (2016): E5052—E5061. http://dx.doi.org/10.1073/pnas.1606656113.

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Bacterial cell division is driven by the divisome, a ring-shaped protein complex organized by the bacterial tubulin homolog FtsZ. Although most of the division proteins inEscherichia colihave been identified, how they assemble into the divisome and synthesize the septum remains poorly understood. Recent studies suggest that the bacterial actin homolog FtsA plays a critical role in divisome assembly and acts synergistically with the FtsQLB complex to regulate the activity of the divisome. FtsEX, an ATP-binding cassette transporter-like complex, is also necessary for divisome assembly and inhibi

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Glas, Marjolein, Eiso AB, Johan Hollander, Gregg Siegal, Joen Luirink, and Iwan de Esch. "Interrogating the Essential Bacterial Cell Division Protein FtsQ with Fragments Using Target Immobilized NMR Screening (TINS)." International Journal of Molecular Sciences 20, no. 15 (2019): 3684. http://dx.doi.org/10.3390/ijms20153684.

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The divisome is a large protein complex that regulates bacterial cell division and therefore represents an attractive target for novel antibacterial drugs. In this study, we report on the ligandability of FtsQ, which is considered a key component of the divisome. For this, the soluble periplasmic domain of Escherichia coli FtsQ was immobilized and used to screen a library of 1501 low molecular weight (< 300 Da), synthetic compounds for those that interact with the protein. A primary screen was performed using target immobilized NMR screening (TINS) and yielded 72 hits. Subsequently, these h

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Yao, Xuanli, Xiangfeng Wang, and Xin Xiang. "FHIP and FTS proteins are critical for dynein-mediated transport of early endosomes in Aspergillus." Molecular Biology of the Cell 25, no. 14 (2014): 2181–89. http://dx.doi.org/10.1091/mbc.e14-04-0873.

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The minus end–directed microtubule motor cytoplasmic dynein transports various cellular cargoes, including early endosomes, but how dynein binds to its cargo remains unclear. Recently fungal Hook homologues were found to link dynein to early endosomes for their transport. Here we identified FhipA in Aspergillus nidulans as a key player for HookA (A. nidulans Hook) function via a genome-wide screen for mutants defective in early-endosome distribution. The human homologue of FhipA, FHIP, is a protein in the previously discovered FTS/Hook/FHIP (FHF) complex, which contains, besides FHIP and Hook

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Ottolenghi, A. C., and J. A. Ayala. "Induction of a class I beta-lactamase from Citrobacter freundii in Escherichia coli requires active ftsZ but not ftsA or ftsQ products." Antimicrobial Agents and Chemotherapy 35, no. 11 (1991): 2359–65. http://dx.doi.org/10.1128/aac.35.11.2359.

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Jensen, S. O., L. S. Thompson, and E. J. Harry. "Cell Division in Bacillus subtilis: FtsZ and FtsA Association Is Z-Ring Independent, and FtsA Is Required for Efficient Midcell Z-Ring Assembly." Journal of Bacteriology 187, no. 18 (2005): 6536–44. http://dx.doi.org/10.1128/jb.187.18.6536-6544.2005.

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ABSTRACT The earliest stage in cell division in bacteria is the assembly of a Z ring at the division site at midcell. Other division proteins are also recruited to this site to orchestrate the septation process. FtsA is a cytosolic division protein that interacts directly with FtsZ. Its function remains unknown. It is generally believed that FtsA localization to the division site occurs immediately after Z-ring formation or concomitantly with it and that FtsA is responsible for recruiting the later-assembling membrane-bound division proteins to the division site. Here, we report the developmen

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Weiner, Barbara, Leo W. Y. Yeung, Erin B. Marchington, Lisa A. D'Agostino, and Scott A. Mabury. "Organic fluorine content in aqueous film forming foams (AFFFs) and biodegradation of the foam component 6 : 2 fluorotelomermercaptoalkylamido sulfonate (6 : 2 FTSAS)." Environmental Chemistry 10, no. 6 (2013): 486. http://dx.doi.org/10.1071/en13128.

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Environmental context Total organofluorine and known fluorosurfactants were quantified in 11 aqueous film forming foams (AFFFs) used to extinguish fires in Ontario, Canada, and one commercial AFFF product. By comparing the concentrations of known fluorosurfactants with the total organofluorine, less than 10% of the fluorosurfactants were identified in half of the samples. Our biodegradation experiment with one of the fluorosurfactants using waste-water treatment plant sludge showed that it was a potential source of perfluoroalkyl carboxylates, which are persistent in the environment. Abstract

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Fujiwara, Kei, and Hideki Taguchi. "Filamentous Morphology in GroE-Depleted Escherichia coli Induced by Impaired Folding of FtsE." Journal of Bacteriology 189, no. 16 (2007): 5860–66. http://dx.doi.org/10.1128/jb.00493-07.

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ABSTRACT The chaperonin GroE (GroEL and the cochaperonin GroES) is the only chaperone system that is essential for the viability of Escherichia coli. It is known that GroE-depleted cells exhibit a filamentous morphology, suggesting that GroE is required for the folding of proteins involved in cell division. Although previous studies, including proteome-wide analyses of GroE substrates, have suggested several targets of GroE in cell division, there is no direct in vivo evidence to identify which substrates exhibit obligate dependence on GroE for folding. Among the candidate substrates, we found

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Zhang, Jing, Zongming Ren, and Meng Chen. "Immunotoxicity and Transcriptome Analyses of Zebrafish (Danio rerio) Embryos Exposed to 6:2 FTSA." Toxics 11, no. 5 (2023): 459. http://dx.doi.org/10.3390/toxics11050459.

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As a new alternative to perfluorooctane sulfonic acid (PFOS), 6:2 fluorotelomer sulfonic acid (6:2 FTSA) has been widely produced and used in recent years, and its concentration and frequency of detection in the aquatic environment and aquatic organisms are increasing. However, studies of its toxicity in aquatic biological systems are alarmingly scarce, and the relevant toxicological information needs to be improved. In this study, we investigated AB wild-type zebrafish (Danio rerio) embryos subjected to acute 6:2 FTSA exposure for immunotoxicity using immunoassays and transcriptomics. Immune

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Demesa-Castañeda, Alba V., David J. Pérez, César Millán-Pacheco, Armando Hernández-Mendoza, and Rodrigo Said Razo-Hernández. "Searching for New Antibacterial Compounds Against Staphylococcus aureus: A Computational Study on the Binding Between FtsZ and FtsA." Drugs and Drug Candidates 3, no. 4 (2024): 751–73. http://dx.doi.org/10.3390/ddc3040043.

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Background: Staphylococcus aureus is a pathogen that has become resistant to different antibiotics, which makes it a threat to human health. Although the first penicillin-resistant strain appeared in 1945, nowadays, there are just a few alternatives to fight it. To circumvent this issue, novel approaches to develop drugs to target proteins of the bacteria cytoskeleton, essential for bacteria’s binary fission, are being developed. FtsZ and FtsA are two proteins that are key for the initial stages of binary fission. On one side, FtsZ forms a polymeric circular structure called the Z ring; meanwh

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Taschner, P. E., P. G. Huls, E. Pas, and C. L. Woldringh. "Division behavior and shape changes in isogenic ftsZ, ftsQ, ftsA, pbpB, and ftsE cell division mutants of Escherichia coli during temperature shift experiments." Journal of Bacteriology 170, no. 4 (1988): 1533–40. http://dx.doi.org/10.1128/jb.170.4.1533-1540.1988.

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Chen, Joseph C., Michael Minev, and Jon Beckwith. "Analysis of ftsQ Mutant Alleles in Escherichia coli: Complementation, Septal Localization, and Recruitment of Downstream Cell Division Proteins." Journal of Bacteriology 184, no. 3 (2002): 695–705. http://dx.doi.org/10.1128/jb.184.3.695-705.2002.

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ABSTRACT FtsQ, a 276-amino-acid, bitopic membrane protein, is one of the nine proteins known to be essential for cell division in gram-negative bacterium Escherichia coli. To define residues in FtsQ critical for function, we performed random mutagenesis on the ftsQ gene and identified four alleles (ftsQ2, ftsQ6, ftsQ15, and ftsQ65) that fail to complement the ftsQ1(Ts) mutation at the restrictive temperature. Two of the mutant proteins, FtsQ6 and FtsQ15, are functional at lower temperatures but are unable to localize to the division site unless wild-type FtsQ is depleted, suggesting that they

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Bottos, Eric M., Ebtihal Y. AL-shabib, Dayton M. J. Shaw, et al. "Transcriptomic response of Gordonia sp. strain NB4-1Y when provided with 6:2 fluorotelomer sulfonamidoalkyl betaine or 6:2 fluorotelomer sulfonate as sole sulfur source." Biodegradation 31, no. 4-6 (2020): 407–22. http://dx.doi.org/10.1007/s10532-020-09917-8.

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Abstract Perfluoroalkyl and polyfluoroalkyl substances (PFAS) are environmental contaminants of concern. We previously described biodegradation of two PFAS that represent components and transformation products of aqueous film-forming foams (AFFF), 6:2 fluorotelomer sulfonamidoalkyl betaine (6:2 FTAB) and 6:2 fluorotelomer sulfonate (6:2 FTSA), by Gordonia sp. strain NB4-1Y. To identify genes involved in the breakdown of these compounds, the transcriptomic response of NB4-1Y was examined when grown on 6:2 FTAB, 6:2 FTSA, a non-fluorinated analog of 6:2 FTSA (1-octanesulfonate), or MgSO4, as sol

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Pilhofer, Martin, Kristina Rappl, Christina Eckl, et al. "Characterization and Evolution of Cell Division and Cell Wall Synthesis Genes in the Bacterial Phyla Verrucomicrobia, Lentisphaerae, Chlamydiae, and Planctomycetes and Phylogenetic Comparison with rRNA Genes." Journal of Bacteriology 190, no. 9 (2008): 3192–202. http://dx.doi.org/10.1128/jb.01797-07.

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ABSTRACT In the past, studies on the relationships of the bacterial phyla Planctomycetes, Chlamydiae, Lentisphaerae, and Verrucomicrobia using different phylogenetic markers have been controversial. Investigations based on 16S rRNA sequence analyses suggested a relationship of the four phyla, showing the branching order Planctomycetes, Chlamydiae, Verrucomicrobia/Lentisphaerae. Phylogenetic analyses of 23S rRNA genes in this study also support a monophyletic grouping and their branching order—this grouping is significant for understanding cell division, since the major bacterial cell division

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Pichoff, Sebastien, Shishen Du, and Joe Lutkenhaus. "Disruption of divisome assembly rescued by FtsN–FtsA interaction inEscherichia coli." Proceedings of the National Academy of Sciences 115, no. 29 (2018): E6855—E6862. http://dx.doi.org/10.1073/pnas.1806450115.

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Cell division requires the assembly of a protein complex called the divisome. The divisome assembles in a hierarchical manner, with FtsA functioning as a hub to connect the Z-ring with the rest of the divisome and FtsN arriving last to activate the machine to synthesize peptidoglycan. FtsEX arrives as the Z-ring forms and acts on FtsA to initiate recruitment of the other divisome components. In the absence of FtsEX, recruitment is blocked; however, a multitude of conditions allow FtsEX to be bypassed. Here, we find that all such FtsEX bypass conditions, as well as the bypass of FtsK, depend up

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Berezuk, Alison M., Elyse J. Roach, Laura Seidel, Reggie Y. Lo, and Cezar M. Khursigara. "FtsA G50E mutant suppresses the essential requirement for FtsK during bacterial cell division in Escherichia coli." Canadian Journal of Microbiology 66, no. 4 (2020): 313–27. http://dx.doi.org/10.1139/cjm-2019-0493.

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In Escherichia coli, the N-terminal domain of the essential protein FtsK (FtsKN) is proposed to modulate septum formation through the formation of dynamic and essential protein interactions with both the Z-ring and late-stage division machinery. Using genomic mutagenesis, complementation analysis, and in vitro pull-down assays, we aimed to identify protein interaction partners of FtsK essential to its function during division. Here, we identified the cytoplasmic Z-ring membrane anchoring protein FtsA as a direct protein–protein interaction partner of FtsK. Random genomic mutagenesis of an ftsK

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Kushwah, Vinita Chauhan, Ritika Chauhan, and Ram Kumar Dhaked. "Fluorescence Thermal Shift Assay based High Through-put Screening in Small Molecule Drug Discovery: A Brief Overview." Journal of Modern Biology and Drug Discovery 3 (May 28, 2024): 3. http://dx.doi.org/10.53964/jmbdd.2024003.

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Background: The Early drug discovery process was majorly phenotypic, lacking target specificity, and mechanism of action causing short and/or long-term toxicological impacts on the patients leading to several drug withdrawals from the market. Biochemical procedures and methods used in drug discovery and development make it lengthy in terms of time requiring approx. 15 years with the investment of billions of dollars for a new drug molecule. Technological advancement leading to the identification of protein structures through crystallography paved a new path toward targeted drug discovery. Obje

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Masters, Millicent, Trevor Paterson, Andrew G. Popplewell, Thomas Owen-Hughes, J. H. Pringle, and Kenneth J. Begg. "The effect of DnaA protein levels and the rate of initiation at oriC on transcription originating in the ftsQ and ftsA genes: In vivo experiments." Molecular and General Genetics MGG 216, no. 2-3 (1989): 475–83. http://dx.doi.org/10.1007/bf00334393.

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Krupka, Marcin, and William Margolin. "Unite to divide: Oligomerization of tubulin and actin homologs regulates initiation of bacterial cell division." F1000Research 7 (February 28, 2018): 235. http://dx.doi.org/10.12688/f1000research.13504.1.

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To generate two cells from one, bacteria such asEscherichia coliuse a complex of membrane-embedded proteins called the divisome that synthesize the division septum. The initial stage of cytokinesis requires a tubulin homolog, FtsZ, which forms polymers that treadmill around the cell circumference. The attachment of these polymers to the cytoplasmic membrane requires an actin homolog, FtsA, which also forms dynamic polymers that directly bind to FtsZ. Recent evidence indicates that FtsA and FtsZ regulate each other’s oligomeric state inE. colito control the progression of cytokinesis, including

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Hale, Cynthia A., and Piet A. J. de Boer. "Recruitment of ZipA to the Septal Ring ofEscherichia coli Is Dependent on FtsZ and Independent of FtsA." Journal of Bacteriology 181, no. 1 (1999): 167–76. http://dx.doi.org/10.1128/jb.181.1.167-176.1999.

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ABSTRACT Cell division in prokaryotes is mediated by the septal ring. InEscherichia coli, this organelle consists of several essential division proteins, including FtsZ, FtsA, and ZipA. To gain more insight into how the structure is assembled, we studied the interdependence of FtsZ, FtsA, and ZipA localization using both immunofluorescence and Gfp tagging techniques. To this end, we constructed a set of strains allowing us to determine the cellular location of each of these three proteins in cells from which one of the other two had been specifically depleted. Our results show that ZipA fails

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El Najjar, Nina, Jihad El Andari, Christine Kaimer, Georg Fritz, Thomas C. Rösch, and Peter L. Graumann. "Single-Molecule Tracking of DNA Translocases inBacillus subtilisReveals Strikingly Different Dynamics of SftA, SpoIIIE, and FtsA." Applied and Environmental Microbiology 84, no. 8 (2018): e02610-17. http://dx.doi.org/10.1128/aem.02610-17.

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ABSTRACTLike many bacteria,Bacillus subtilispossesses two DNA translocases that affect chromosome segregation at different steps. Prior to septum closure, nonsegregated DNA is moved into opposite cell halves by SftA, while septum-entrapped DNA is rescued by SpoIIIE. We have used single-molecule fluorescence microscopy and tracking (SMT) experiments to describe the dynamics of the two different DNA translocases, the cell division protein FtsA and the glycolytic enzyme phosphofructokinase (PfkA), in real time. SMT revealed that about 30% of SftA molecules move through the cytosol, while a fracti

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Maurya, Ganesh K., Kruti Modi, Manisha Banerjee, Reema Chaudhary, Yogendra S. Rajpurohit, and Hari S. Misra. "Phosphorylation of FtsZ and FtsA by a DNA Damage-Responsive Ser/Thr Protein Kinase Affects Their Functional Interactions in Deinococcus radiodurans." mSphere 3, no. 4 (2018): e00325-18. http://dx.doi.org/10.1128/msphere.00325-18.

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ABSTRACT Deinococcus radiodurans, a highly radioresistant bacterium, does not show LexA-dependent regulation of recA expression in response to DNA damage. On the other hand, phosphorylation of DNA repair proteins such as PprA and RecA by a DNA damage-responsive Ser/Thr protein kinase (STPK) (RqkA) could improve their DNA metabolic activities as well as their roles in the radioresistance of D. radiodurans. Here we report RqkA-mediated phosphorylation of cell division proteins FtsZ and FtsA in vitro and in surrogate Escherichia coli bacteria expressing RqkA. Mass spectrometric analysis mapped se

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Chon, Younghae, and Randall Gayda. "Studies with FtsA-LacZ protein fusions reveal FtsA located inner-outer membrane junctions." Biochemical and Biophysical Research Communications 152, no. 3 (1988): 1023–30. http://dx.doi.org/10.1016/s0006-291x(88)80386-3.

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Yim, Lucía, Guy Vandenbussche, Jesús Mingorance, et al. "Role of the Carboxy Terminus of Escherichia coli FtsA in Self-Interaction and Cell Division." Journal of Bacteriology 182, no. 22 (2000): 6366–73. http://dx.doi.org/10.1128/jb.182.22.6366-6373.2000.

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ABSTRACT The role of the carboxy terminus of the Escherichia coli cell division protein FtsA in bacterial division has been studied by making a series of short sequential deletions spanning from residue 394 to 420. Deletions as short as 5 residues destroy the biological function of the protein. Residue W415 is essential for the localization of the protein into septal rings. Overexpression of theftsA alleles harboring these deletions caused a coiled cell phenotype previously described for another carboxy-terminal mutation (Gayda et al., J. Bacteriol. 174:5362–5370, 1992), suggesting that an int

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Tamura, Masaru, Kangseok Lee, Christine A. Miller, et al. "RNase E Maintenance of Proper FtsZ/FtsA Ratio Required for Nonfilamentous Growth of Escherichia coli Cells but Not for Colony-Forming Ability." Journal of Bacteriology 188, no. 14 (2006): 5145–52. http://dx.doi.org/10.1128/jb.00367-06.

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ABSTRACT Inactivation or deletion of the RNase E-encoding rne gene of Escherichia coli results in the growth of bacterial cells as filamentous chains in liquid culture (K. Goldblum and D. Apirion, J. Bacteriol. 146:128-132, 1981) and the loss of colony-forming ability (CFA) on solid media. RNase E dysfunction is also associated with abnormal processing of ftsQAZ transcripts (K. Cam, G. Rome, H. M. Krisch, and J.-P. Bouché, Nucleic Acids Res. 24:3065-3070, 1996), which encode proteins having a central role in septum formation during cell division. We show here that RNase E regulates the relati

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