The Mechanics of FtsZ Fibers [PDF]
Biophysical Journal, 2012 Inhibition of the Fts family of proteins causes the growth of long filamentous cells, indicating that they play some role in cell division. FtsZ polymerizes into protofilaments and assembles into the Z-ring at the future site of the septum of cell division.
Turner, Daniel J. +6 more
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NDK Interacts with FtsZ and Converts GDP to GTP to Trigger FtsZ Polymerisation--A Novel Role for NDK. [PDF]
PLoS ONE, 2015 Nucleoside diphosphate kinase (NDK), conserved across bacteria to humans, synthesises NTP from NDP and ATP. The eukaryotic homologue, the NDPK, uses ATP to phosphorylate the tubulin-bound GDP to GTP for tubulin polymerisation.
Saurabh Mishra +7 more
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FtsZ dimerization in vivo [PDF]
Molecular Microbiology, 1999 A hybrid assay, based on the properties of the λ repressor, was developed to detect FtsZ dimerization in Escherichia coli in vivo. A gene fusion comprising the N‐terminal end of the λcI repressor gene and the complete E. coli ftsZ gene was constructed. The fused protein resulted in a functional λ repressor and was able to complement the thermosensitive
DI LALLO, GUSTAVO +3 more
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Characterization of the FtsZ C-Terminal Variable (CTV) Region in Z-Ring Assembly and Interaction with the Z-Ring Stabilizer ZapD in E. coli Cytokinesis. [PDF]
PLoS ONE, 2016 Polymerization of a ring-like cytoskeletal structure, the Z-ring, at midcell is a highly conserved feature in virtually all bacteria. The Z-ring is composed of short protofilaments of the tubulin homolog FtsZ, randomly arranged and held together through ...
Kuo-Hsiang Huang +3 more
doaj +1 more source
eLife, 2021 Bacterial cell division is driven by the polymerization of the GTPase FtsZ into a contractile structure, the so-called Z-ring. This essential process involves proteins that modulate FtsZ dynamics and hence the overall Z-ring architecture.
Félix Ramos-León +7 more
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Interactions between heterologous FtsA and FtsZ proteins at the FtsZ ring [PDF]
Journal of Bacteriology, 1997 FtsZ and FtsA are essential for cell division in Escherichia coli and colocalize to the septal ring. One approach to determine what regions of FtsA and FtsZ are important for their interaction is to identify in vivo interactions between FtsA and FtsZ from different species.
X, Ma +5 more
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Thermal adaptation of mesophilic and thermophilic FtsZ assembly by modulation of the critical concentration. [PDF]
PLoS ONE, 2017 Cytokinesis is the last stage in the cell cycle. In prokaryotes, the protein FtsZ guides cell constriction by assembling into a contractile ring-shaped structure termed the Z-ring.
Luis Concha-Marambio +4 more
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The Nucleoid Occlusion SlmA Protein Accelerates the Disassembly of the FtsZ Protein Polymers without Affecting Their GTPase Activity. [PDF]
PLoS ONE, 2015 Division site selection is achieved in bacteria by different mechanisms, one of them being nucleoid occlusion, which prevents Z-ring assembly nearby the chromosome. Nucleoid occlusion in E.
Elisa J Cabré +8 more
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ZipA Uses a Two-Pronged FtsZ-Binding Mechanism Necessary for Cell Division
mBio, 2021 In most bacteria, cell division is centrally organized by the FtsZ protein, which assembles into dynamic filaments at the division site along the cell membrane that interact with other key cell division proteins.
Todd A. Cameron +4 more
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SepG coordinates sporulation-specific cell division and nucleoid organization in Streptomyces coelicolor [PDF]
Open Biology, 2016 Bacterial cell division is a highly complex process that requires tight coordination between septum formation and chromosome replication and segregation.
Le Zhang +3 more
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