ZipA binds to FtsZ with high affinity and enhances the stability of FtsZ protofilaments. [PDF]
PLoS 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 +4 more sources
ZapA uses a two‐pronged mechanism to facilitate Z ring formation in Escherichia coli [PDF]
mLifeThe 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
ZapC crosslinks FtsZ filaments through a dual-binding mechanism modulated by the intrinsically disordered linker of FtsZ in Escherichia coli [PDF]
mBioMost 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 +2 more sources
Mycobacterium tuberculosis ClpX interacts with FtsZ and interferes with FtsZ assembly.
PLoS ONE, 2010 FtsZ assembly at the midcell division site in the form of a Z-ring is crucial for initiation of the cell division process in eubacteria. It is largely unknown how this process is regulated in the human pathogen Mycobacterium tuberculosis.
Renata Dziedzic +9 more
doaj +3 more sources
Frontiers in Microbiology, 2018 Filamentous cyanobacteria grow by intercalary cell division, which should involve distinct steps compared to those producing separate daughter cells. The N-terminal region of FtsZ is highly conserved in the clade of filamentous cyanobacteria capable of ...
Laura Corrales-Guerrero +2 more
exaly +3 more sources
FtsZ forms biomolecular condensates in a polar-growing Alphaproteobacterium [PDF]
mBioThe 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
FtsZ contributes to cytoadhesion and interaction with host extracellular matrix components and plasminogen in Mycoplasma bovis [PDF]
Veterinary ResearchMycoplasma 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
FtsZ placement in nucleoid-free bacteria.
PLoS ONE, 2014 We describe the placement of the cytoplasmic FtsZ protein, an essential component of the division septum, in nucleoid-free Escherichia coli maxicells. The absence of the nucleoid is accompanied in maxicells by degradation of the SlmA protein.
Manuel Pazos +5 more
doaj +5 more sources
Structural basis for the interaction between the bacterial cell division proteins FtsZ and ZapA [PDF]
Nature CommunicationsCell division in most bacteria is regulated by the tubulin homolog FtsZ as well as ZapA, a FtsZ-associated protein. However, how FtsZ and ZapA function coordinately has remained elusive.
Junso Fujita +10 more
doaj +2 more sources
Antistaphylococcal Activity of the FtsZ Inhibitor C109 [PDF]
Pathogens, 2021 Staphylococcus aureus infections represent a great concern due to their versatility and involvement in different types of diseases. The shortage of available clinical options, especially to treat multiresistant strains, makes the discovery of new effective compounds essential.
Gabriele Trespidi +10 more
openaire +5 more sources