Results 41 to 50 of about 9,319 (176)
mBio, 2022 FtsZ filaments are the major structural component of the bacterial Z ring and are drivers of bacterial division. Crystal structures for FtsZ from some Gram-positive bacteria in the presence of GTP analogs suggest the possibility of a high-energy, “tense”
Kelsey M. McCoy +2 more
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FtsZ Polymerization Assays: Simple Protocols and Considerations [PDF]
Journal of Visualized Experiments, 2013 During bacterial cell division, the essential protein FtsZ assembles in the middle of the cell to form the so-called Z-ring. FtsZ polymerizes into long filaments in the presence of GTP in vitro, and polymerization is regulated by several accessory proteins.
Król, Ewa, Scheffers, Dirk-Jan
openaire +3 more sources
RATEX: A Scalable RNA‐Based Platform for Logical and Multi‐Layered Cellular Programming
Angewandte Chemie, Volume 138, Issue 26, 22 June 2026.RATEX integrated ribosome‐mediated transcription control with synthetic RNA regulators, enabling simultaneous processing of RNA, metabolite, and small‐molecule inputs through complex logic operations within a single transcript. The platform achieves up to 1,492‐fold gene regulation, multi‐input hybrid logic gates, RNA‐programmed signaling cascades, and
Hyunseop Goh +3 more
wiley +2 more sources
FtsZ-Dependent Elongation of a Coccoid Bacterium [PDF]
mBio, 2016 ABSTRACT A mechanistic understanding of the determination and maintenance of the simplest bacterial cell shape, a sphere, remains elusive compared with that of more complex shapes. Cocci seem to lack a dedicated elongation machinery, and a spherical shape has been considered an evolutionary dead-end morphology, as a transition ...
Pereira, Ana R. +14 more
openaire +7 more sources
Structures of a FtsZ single protofilament and a double-helical tube in complex with a monobody
Nature Communications, 2023 FtsZ polymerizes into protofilaments to form the Z-ring that acts as a scaffold for accessory proteins during cell division. Structures of FtsZ have been previously solved, but detailed mechanistic insights are lacking.
Junso Fujita +12 more
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Antibiotics, 2020 The inhibition of a bacterial cell division protein, filamentous temperature-sensitive Z (FtsZ), prevents the reproduction of Mycobacteria. To propose potent inhibitors of FtsZ, the binding properties of FtsZ with various derivatives of Zantrin ZZ3 were ...
Shohei Yamamoto +7 more
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Genetic and biochemical characterization of the MinC-FtsZ interaction in Bacillus subtilis. [PDF]
PLoS ONE, 2013 Cell division in bacteria is regulated by proteins that interact with FtsZ and modulate its ability to polymerize into the Z ring structure. The best studied of these regulators is MinC, an inhibitor of FtsZ polymerization that plays a crucial role in ...
Valdir Blasios +7 more
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A Screening Model of Antibacterial Agents Based on Escherichia coli Cell-Division Protein
Applied Sciences, 2023 Pathogenic Escherichia coli cannot be killed by most antibiotics (including colistin, a last-resort drug) due to the rapid development of antibiotic resistance.
Qiuyu Fan +5 more
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mBio, 2020 A microfluidic system coupled with fluorescence microscopy is a powerful approach for quantitative analysis of bacterial growth. Here, we measure parameters of growth and dynamic localization of the cell division initiation protein FtsZ in Bacillus ...
Yuanchen Yu +5 more
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A Polymerization-Associated Structural Switch in FtsZ That Enables Treadmilling of Model Filaments
mBio, 2017 Bacterial cell division in many organisms involves a constricting cytokinetic ring that is orchestrated by the tubulin-like protein FtsZ. FtsZ forms dynamic filaments close to the membrane at the site of division that have recently been shown to ...
James M. Wagstaff +6 more
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