Results 1 to 10 of about 9,319 (176)

Proteolysis-Dependent Remodeling of the Tubulin Homolog FtsZ at the Division Septum in Escherichia coli. [PDF]

PLoS ONE, 2017
During bacterial cell division a dynamic protein structure called the Z-ring assembles at the septum. The major protein in the Z-ring in Escherichia coli is FtsZ, a tubulin homolog that polymerizes with GTP.
Marissa G Viola, Christopher J LaBreck, Joseph Conti, Jodi L Camberg   +3 more
doaj   +1 more source

Location of dual sites in E. coli FtsZ important for degradation by ClpXP; one at the C-terminus and one in the disordered linker.

PLoS ONE, 2014
ClpXP is a two-component ATP-dependent protease that unfolds and degrades proteins bearing specific recognition signals. One substrate degraded by Escherichia coli ClpXP is FtsZ, an essential cell division protein.
Jodi L Camberg, Marissa G Viola, Leslie Rea, Joel R Hoskins, Sue Wickner   +4 more
doaj   +1 more source

A canonical FtsZ protein in Verrucomicrobium spinosum, a member of the Bacterial phylum Verrucomicrobia that also includes tubulin-producing Prosthecobacter species

BMC Evolutionary Biology, 2007
Background The origin and evolution of the homologous GTP-binding cytoskeletal proteins FtsZ typical of Bacteria and tubulin characteristic of eukaryotes is a major question in molecular evolutionary biology. Both FtsZ and tubulin are central to key cell
Staley James T, Oakley Brian, Lafi Feras F, Yee Benjamin, Fuerst John A   +4 more
doaj   +1 more source

ZipA and FtsA* stabilize FtsZ-GDP miniring structures

Scientific Reports, 2017
The cytokinetic division ring of Escherichia coli comprises filaments of FtsZ tethered to the membrane by FtsA and ZipA. Previous results suggested that ZipA is a Z-ring stabilizer, since in vitro experiments it is shown that ZipA enhanced FtsZ assembly ...
Yaodong Chen, Haiyan Huang, Masaki Osawa, Harold P. Erickson   +3 more
doaj   +1 more source

Antibacterial activity of alkyl gallates is a combination of direct targeting of FtsZ and permeabilization of bacterial membranes

Frontiers in Microbiology, 2015
Alkyl gallates are compounds with reported antibacterial activity. One of the modes of action is binding of the alkyl gallates to the bacterial membrane and interference with membrane integrity.
Ewa eKról, Anabela ede Sousa Borges, Isabel eda Silva, Carlos Roberto Polaquini, Luis Octavio Regasini, Henrique eFerreira, Dirk-Jan eScheffers   +6 more
doaj   +1 more source

Phosphorylation of FtsZ and FtsA by a DNA Damage-Responsive Ser/Thr Protein Kinase Affects Their Functional Interactions in Deinococcus radiodurans

mSphere, 2018
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 ...
Ganesh K. Maurya, Kruti Modi, Manisha Banerjee, Reema Chaudhary, Yogendra S. Rajpurohit, Hari S. Misra   +5 more
doaj   +1 more source

Unveiling Berberine analogues as potential inhibitors of Escherichia coli FtsZ through machine learning molecular docking and molecular dynamics approach

Scientific Reports
The bacterial cell division protein FtsZ, a crucial GTPase, plays a vital role in the formation of the contractile Z-ring, which is essential for bacterial cytokinesis.
Aditi Roy, Anand Anbarasu
doaj   +1 more source

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

Antibiotics
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, Alessia Lanzini, Valentina Straniero, William Margolin   +3 more
doaj   +1 more source

N-terminus GTPase domain of the cytoskeleton protein FtsZ plays a critical role in its adaptation to high hydrostatic pressure

Frontiers in Microbiology
Studies in model microorganisms showed that cell division is highly vulnerable to high hydrostatic pressure (HHP). Disassembly of FtsZ filaments induced by HHP results in the failure of cell division and formation of filamentous cells in E. coli.
Xue-Hua Cui, Xue-Hua Cui, Yu-Chen Wei, Xue-Gong Li, Xue-Gong Li, Xiao-Qing Qi, Xiao-Qing Qi, Long-Fei Wu, Long-Fei Wu, Long-Fei Wu, Wei-Jia Zhang, Wei-Jia Zhang   +11 more
doaj   +1 more source

Molecular dynamics simulations reveal differences in the conformational stability of FtsZs derived from Staphylococcus aureus and Bacillus subtilis

Scientific Reports
FtsZ is highly conserved among bacteria and plays an essential role in bacterial cell division. The tense conformation of FtsZ bound to GTP assembles into a straight filament via head-to-tail associations, and then the upper subunit of FtsZ hydrolyzes ...
Taichi Takasawa, Takashi Matsui, Go Watanabe, Yoshio Kodera   +3 more
doaj   +1 more source