ftsZ Antibody

1. Efficient models of polymerization applied to FtsZ ring assembly in Escherichia coli. PMID: 29686085
2. FtsZ E237 and E241 are critical amino acids that affect the amphipathic helix characteristics of FtsZ (236-245) domain, FtsZ assembly and FtsZ-FtsA interaction in E. coli strains. PMID: 29756735
3. the presence of FtsN always correlated with membrane invagination, indicating that allosteric activation of peptidoglycan ingrowth is the trigger for constriction of the cell envelope during cell division in E. coli. PMID: 27609565
4. Although several other protein modulators are known to target FtsZ, the CbtA-interacting surface we identify represents a novel inhibitory target. Our findings establish CbtA as a dual function toxin that inhibits both cell division and cell elongation via direct and independent interactions with FtsZ and MreB. PMID: 28931012
5. MreB is not recruited to the FtsZ ring in secA mutant cells, contributing to division arrest and cell filamentation.. Thus, when we reroute RodZ, MreB membrane-anchor, by fusing it to a SecA-independent integral membrane protein and overproducing it, MreB localization is restored and the defect in cell division is corrected. PMID: 28945742
6. FtsZ treadmilling provides a mechanism for achieving uniform septal cell wall synthesis to enable correct polar morphology. PMID: 28209899
7. ZapD acts as a molecular cross-linking reagent between FtsZ protofilaments to enhance FtsZ assembly PMID: 28100778
8. Residues R56, R221, and R225 of zapD are important for bundling FtsZ filaments. PMID: 27021560
9. These results suggest that the in vivo organization of the Z-ring is largely dependent on the intrinsic polymerization properties of FtsZ, which are significantly influenced by the GTPase activity and concentration of FtsZ. PMID: 27310678
10. FtsZ protein interaction domains and motifs with GP0.4 protein from bacteriophage T7 provide target sites for antibacterial drug design. PMID: 27411831
11. Combined, these data reveal the molecular basis for the SlmA-DNA-FtsZ interaction with implications for SlmA's NO function and underscore the ability of the FtsZ CTD to adopt a wide range of conformations, explaining its ability to bind diverse regulatory proteins. PMID: 27091999
12. E75, R78 and D82 of FtsZ are key residues for FtsZ self-assembly and FtsZ-MreB interaction. PMID: 27373074
13. These data suggest that FtsZ, and potentially other enzymes whose assembly is similarly regulated, can compensate for defects in catalysis through increases in substrate binding and subunit-subunit interactions. PMID: 26463348
14. ZapC binds the large FtsZ globular core rather than C-terminal tail, and the presence of two adjacent pockets suggests possible mechanisms for ZapC-mediated FtsZ bundling PMID: 26655719
15. Work highlighted the importance of FtsZ protofilament bundling during cell division and its likely role in regulating additional divisome activities. PMID: 26046682
16. Decrease in FtsZ concentration in the ppGpp(0) strain makes cell division vulnerable to SulA inhibition. PMID: 26644431
17. New data was obtained that support the hypothesis that the Z-ring is a spiral structure that constricts during division, assisting the formation of the septum between daughter cells. PMID: 27012097
18. The present study suggests the presence of a novel binding site in FtsZ that interacts with the small molecules and can be targeted for the screening and development of new antibacterial agents PMID: 26285656
19. In the process of E. coli cell division, MinC-MinD copolymers bind to membrane, interact with FtsZ, and are disassembled by MinE. PMID: 25500731
20. Architecture of the ring formed by the tubulin homologue FtsZ in bacterial cell division has been described. PMID: 25490152
21. findings show that the oligomerization of FtsZ converts the CCTP (conserved carboxy-terminal peptide) to a multivalent ligand that binds multiple ZipAs bound to a surface with high avidity PMID: 25382687
22. Phytochemicals as inhibitors of bacterial cell division protein FtsZ: coumarins are promising candidates PMID: 25062781
23. biomolecular crowding has a considerable effect on the FtsZ dimerization by increasing the dimerization rate constant from 2.6x10(7)M(-1)s(-1) in the absence of crowders to 1.0x10(8)M(-1)s(-1) at crowding level of 0.30. PMID: 25218002
24. these results lead to a model in which SlmA binding to an SBS is activated to bind the tail of FtsZ resulting in further interaction with FtsZ leading to depolymerization of FtsZ polymers. PMID: 25078077
25. Evidence shows that FtsZ departs from the septum before the cytoplasmic compartment has been separated in E. coli. PMID: 24506818
26. Authors found that ZapE is recruited to the Z-ring during late stages of the cell division process and correlates with constriction of the Z-ring. PMID: 24595368
27. These results suggest that the main function of ZapA and ZapB in vivo may not be to promote the association of individual protofilaments but to align FtsZ clusters that consist of multiple FtsZ protofilaments. PMID: 23859153
28. findings suggest that the Z-ring may consist of a percolating network of FtsZ filaments PMID: 23848262
29. The highly conserved negative charge of glutamate 83 and the positive charge of arginine 85 located in the helix H3 bend of FtsZ are required for in vitro FtsZ lateral and longitudinal interactions, respectively and for in vivo cell division. PMID: 23384248
30. Synthetic lethal protein with a defective Min system (SlmA) helps mediate nucleoid occlusion, which prevents chromosome fragmentation by binding FtsZ and inhibiting Z-ring formation. PMID: 23754405
31. analysis of membrane reconstitution of FtsZ-ZipA complex inside giant spherical vesicles made of E. coli lipids PMID: 23149342
32. We generated a number of mutant forms of ZapA with the aim of disrupting the dimer-dimer interface. We show that one of these mutants, I83E, is fully folded and binds to FtsZ, but is a constitutive dimer. PMID: 23098212
33. YeeU was found to directly interact with MreB and FtsZ, and enhance the bundling of their filamentous polymers in vitro and proposed to rename as CbeA for cytoskeleton bundling-enhancing factor A. PMID: 22515815
34. Biochemical evidence indicates that ZapD directly interacts with FtsZ and promotes bundling of FtsZ protofilaments. PMID: 22505682
35. Depolymerization rate is affected both by nucleotide hydrolysis rate and by its exchange along the filament; monomer interfaces are equally competent for hydrolysis, although depolymerization is faster at the open ends than in central filament.[ PMID: 22566654
36. ZipA binds to FtsZ with high affinity and enhances the stability of FtsZ protofilaments PMID: 22164258
37. Escherichia coli cell division protein ZipA forms homodimers prior to association with FtsZ PMID: 22304478
38. obtain ring- and arc-shaped aggregations of FtsZ polymers on the membrane as a function of monomer numbers in the cell PMID: 21335646
39. Together, our results suggested that ClpXP modulates cell division through degradation of FtsZ and possibly other cell division components that function downstream of FtsZ ring assembly. PMID: 21317324
40. The authors show that YeeV toxin inhibits cell division, leads to a change in morphology and lysis of Escherichia coli cells via interaction with two essential cytoskeleton proteins, FtsZ and MreB. PMID: 21166897
41. FtsZ and ZapA interact at the Z rings in vivo. PMID: 20969647
42. The Z-ring of FtsZ adopts a novel compressed helical conformation with variable helical length and pitch. PMID: 20856929
43. Taken together, these data indicate that polar Z rings are more susceptible to MinC/MinD than internal Z rings, even when MinE is absent. PMID: 21097625
44. Based on the results, an updated model for the action of MinC on FtsZ is proposed: MinC interacts with FtsZ to disrupt two interactions, FtsZ-FtsA/ZipA and FtsZ-FtsZ, both of which are essential for Z ring formation. PMID: 20132438
45. FtsZ fiber bundling is triggered by a conformational change in bound GTP PMID: 15328358
46. Results describe the GTP-mediated assembly of FtsZ from Escherichia coli. PMID: 15684053
47. biochemical analysis of FtsZ turnover and GTP hydrolysis in vitro PMID: 15826938
48. Deuterium oxide promotes assembly and bundling of FtsZ protofilaments by increasing hydrophobic interactions between the protofilaments. PMID: 16245323
49. Results describe the activation of FtsZ by monovalent cations. PMID: 16930599
50. The putative Escherichia coli ZapA orthologue, YgfE, exists in a dimer/tetramer equilibrium in solution, binds to FtsZ polymers, strongly promotes FtsZ polymer bundling and is a potent inhibitor of the FtsZ GTPase activity. PMID: 17428494

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KEGG: ecj:JW0093

STRING: 316385.ECDH10B_0077