Results 101 to 110 of about 14,243 (169)

FtsZ mutant measurements.

, 2013
FtsZ mutant measurements.
Jefferson Bettini (399781), Patricia Castellen (399779), Ana Carolina M. Zeri (399783), Rodrigo V. Portugal (399782), Alexandre W. Bisson-Filho (399778), Valdir Blasios (399777), Frederico J. Gueiros-Filho (399784), Maria Luiza C. Nogueira (399780)   +7 more
core   +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

Morphologies of polymeric assemblies of FtsZ and FtsZ CTV mutant proteins.

, 2016
In vitro reactions containing FtsZ and FtsZ CTV mutants (5 ∝M) alone or combined with purified ZapD at 1:1 ratios in a polymerization buffer (50 mM K-MOPS pH 6.5, 50 mM KCl, 2.5 mM MgCl2, and 1 mM GTP) were incubated for 5 mins at room temperature.
Aaron Mychack (2614525), Kuo-Hsiang Huang (2614528), Lukasz Tchorzewski (2614522), Anuradha Janakiraman (2614519)   +3 more
core   +1 more source

Surface-Enhanced Raman Scattering-Based Detection of the Interactions between the Essential Cell Division FtsZ Protein and Bacterial Membrane Elements

, 2012
Surface-enhanced Raman scattering (SERS) spectroscopy has been applied to detect the interaction of the FtsZ protein from Escherichia coli, an essential component of the bacterial division machinery, with either a soluble variant of the ZipA protein ...
Liz-Marzán, Luis, Rivas, Germán, Liz-Marzán, Luis M., Álvarez-Puebla, Ramón A, Ahijado-Guzmán, Rubén, Gómez-Puertas, Paulino, Alvarez-Puebla, Ramón A., Ahijado Guzmán, Rubén   +7 more
core   +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

Borrelia Burgdorferi ftsZ Plays a Role in Cell Division

, 2006
ftsZ is essential for cell division in many microorganisms. In Escherichia coli and Bacillus subtilis, FtsZ plays a role in ring formation at the leading edge of the cell division septum.
Godfrey, Henry P., Dubytska, Lydia, Cabello, Felipe C.   +2 more
core   +1 more source

CalA, a cyAbrB protein, binds to the upstream region of ftsZ and is down-regulated in heterocysts in Anabaena sp PCC 7120

, 2010
A protein of cyAbrB family of regulators, Alr0946 (CalA), was identified by DNA affinity chromatography using DNA fragments from the promoter region of ftsZ in Anabaena/Nostoc sp. PCC 7120.
Xu, XD, Chinese Acad Sci, State Key Lab Freshwater Ecol & Biotechnol, Inst Hydrobiol, Wuhan 430072, Hubei, Peoples R China, Xu, Xudong, He, Dongli   +2 more
core  

Growth rate-dependent regulation of medial FtsZ ring formation

, 2003
FtsZ is an essential cell division protein conserved throughout the bacteria and archaea. In response to an unknown cell cycle signal, FtsZ polymerizes into a ring that establishes the future division site.
Richard B. Weart, Petra Anne Levin
core  

Defining the order of assembly of the <i>Clostridioides difficile</i> divisome complex. [PDF]

J Bacteriol
Harrison GA, Kuhn P, Shrestha S, Caballero Blanco P, Havey L, Shen A.   +5 more
europepmc   +1 more source

Automated synthetic cell-based screening for designed proteins with emergent functions. [PDF]

Nat Commun
Al Nahas K, Frohn BP, Šakanović A, Siedler F, Schwille P.   +4 more
europepmc   +1 more source