Results 1 to 10 of about 14,243 (169)

ZapC crosslinks FtsZ filaments through a dual-binding mechanism modulated by the intrinsically disordered linker of FtsZ in Escherichia coli [PDF]

open access: yesmBio
Most bacteria divide through binary fission, which is mediated by a large protein complex called the divisome. Assembly of the divisome is initiated by the formation of a Z-ring at midcell consisting of polymers of the bacterial tubulin FtsZ. A series of
Ying Li   +6 more
doaj   +3 more sources

ZipA binds to FtsZ with high affinity and enhances the stability of FtsZ protofilaments. [PDF]

open access: yesPLoS ONE, 2011
A bacterial membrane protein ZipA that tethers FtsZ to the membrane is known to promote FtsZ assembly. In this study, the binding of ZipA to FtsZ was monitored using fluorescence spectroscopy.
Anuradha Kuchibhatla   +2 more
doaj   +2 more sources

Visualization of the chloroplast MinE ring in living mesophyll cells of Arabidopsis thaliana [PDF]

open access: yesPlant Signaling & Behavior
Chloroplast division is a complex process influenced by various proteins, among which bacteria-derived MinE plays a vital role in correctly placing the FtsZ-based division apparatus and initiating the division.
Makoto T. Fujiwara, Ryuuichi D. Itoh
doaj   +2 more sources

ZapA uses a two‐pronged mechanism to facilitate Z ring formation in Escherichia coli [PDF]

open access: yesmLife
The tubulin‐like protein FtsZ assembles into the Z ring that leads to the assembly and activation of the division machinery in most bacteria. ZapA, a widely conserved protein that interacts with FtsZ, plays a pivotal role in organizing FtsZ filaments ...
Yuanyuan Cui   +10 more
doaj   +2 more sources

NDK Interacts with FtsZ and Converts GDP to GTP to Trigger FtsZ Polymerisation--A Novel Role for NDK. [PDF]

open access: yesPLoS 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
doaj   +2 more sources

FtsZ forms biomolecular condensates in a polar-growing Alphaproteobacterium [PDF]

open access: yesmBio
The conserved tubulin homolog FtsZ assembles into GTP-dependent protofilaments that organize the bacterial cell division machinery. Purified Escherichia coli FtsZ (FtsZEc) can form biomolecular condensates in the absence of GTP in macromolecular crowding
Todd A. Cameron   +4 more
doaj   +2 more sources

Mechanistic Insights into the Antimicrobial Effect of Benzodioxane-Benzamides Against Escherichia coli [PDF]

open access: yesAntibiotics
Background/Objectives: The bacterial cell division machinery is emerging as an attractive target for antimicrobial compounds. FtsZ, a highly conserved essential division protein, is the target for a number of small molecules such as benzamides.
Lorenzo Suigo   +3 more
doaj   +2 more sources

FtsZ contributes to cytoadhesion and interaction with host extracellular matrix components and plasminogen in Mycoplasma bovis [PDF]

open access: yesVeterinary Research
Mycoplasma bovis causes serious diseases in cattle and is one of the most economically important pathogens threatening the global cattle industry. It is still a great challenge to prevent and control M.
Shanyu Jin   +9 more
doaj   +2 more sources

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]

open access: yesPLoS 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

A conserved cell division protein directly regulates FtsZ dynamics in filamentous and unicellular actinobacteria

open access: yeseLife, 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
doaj   +1 more source

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