Browsing by Author "Osawa, Masaki"
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Cell division without FtsZ--a variety of redundant mechanisms.
(Molecular microbiology, 2010-10)Until 1998 it looked like all bacteria and archaea used a universal cytokinetic machine based on FtsZ. A dozen completely sequenced bacterial genomes all had an ftsZ gene, as did the several sequenced archaeal genomes. Then ... -
Chapter 1 - Tubular liposomes with variable permeability for reconstitution of FtsZ rings.
(Methods in enzymology, 2009-01)We have developed a system for producing tubular multilamellar liposomes that incorporate the protein FtsZ on the inside. We start with a mixture of spherical multilamellar liposomes with FtsZ initially on the outside. Shearing ... -
Curved FtsZ protofilaments generate bending forces on liposome membranes.
(The EMBO journal, 2009-11)We have created FtsZ-YFP-mts where an amphipathic helix on the C-terminus tethers FtsZ to the membrane. When incorporated inside multi-lamellar tubular liposomes, FtsZ-YFP-mts can assemble Z rings that generate a constriction ... -
FtsZ in bacterial cytokinesis: cytoskeleton and force generator all in one.
(Microbiology and molecular biology reviews : MMBR, 2010-12)FtsZ, a bacterial homolog of tubulin, is well established as forming the cytoskeletal framework for the cytokinetic ring. Recent work has shown that purified FtsZ, in the absence of any other division proteins, can assemble ... -
FtsZ Protofilament Curvature Is the Opposite of Tubulin Rings.
(Biochemistry, 2016-07)FtsZ protofilaments (pfs) form the bacterial cytokinetic Z ring. Previous work suggested that a conformational change from straight to curved pfs generated the constriction force. In the simplest model, the C-terminal membrane ... -
Inside-out Z rings--constriction with and without GTP hydrolysis.
(Molecular microbiology, 2011-07)The bacterial tubulin homologue FtsZ forms a ring-like structure called the Z ring that drives cytokinesis. We showed previously that FtsZ-YFP-mts, which has a short amphipathic helix (mts) on its C terminus that inserts ... -
L form bacteria growth in low-osmolality medium.
(Microbiology (Reading, England), 2019-08)L form bacteria do not have a cell wall and are thought to require medium of high osmolality for survival and growth. In this study we tested whether L forms can adapt to growth in lower osmolality medium. We first tested ... -
Liposome division by a simple bacterial division machinery.
(Proceedings of the National Academy of Sciences of the United States of America, 2013-07)We previously reconstituted Z rings in tubular multilamellar liposomes with FtsZ-YFP-mts, where mts is a membrane-targeting amphiphilic helix. These reconstituted Z rings generated a constriction force but did not divide ... -
Negative-stain electron microscopy of inside-out FtsZ rings reconstituted on artificial membrane tubules show ribbons of protofilaments.
(Biophysical journal, 2012-07)FtsZ, the primary cytoskeletal element of the Z ring, which constricts to divide bacteria, assembles into short, one-stranded filaments in vitro. These must be further assembled to make the Z ring in bacteria. Conventional ... -
Probing for Binding Regions of the FtsZ Protein Surface through Site-Directed Insertions: Discovery of Fully Functional FtsZ-Fluorescent Proteins.
(J Bacteriol, 2017-01-01)FtsZ, a bacterial tubulin homologue, is a cytoskeletal protein that assembles into protofilaments that are one subunit thick. These protofilaments assemble further to form a "Z ring" at the center of prokaryotic cells. The ... -
The cell division protein MinD from Pseudomonas aeruginosa dominates the assembly of the MinC-MinD copolymers.
(The Journal of biological chemistry, 2018-04-02)Cell division of rod-shaped bacteria requires the Z ring, a ring of FtsZ filaments associated with the inner-membrane wall. The MinCDE proteins help localize the Z ring to the center of the Escherichia coli cell. MinC, which ... -
The Chloroplast Tubulin Homologs FtsZA and FtsZB from the Red Alga Galdieria sulphuraria Co-assemble into Dynamic Filaments.
(J Biol Chem, 2017-02-07)FtsZ is a homolog of eukaryotic tubulin and is present in almost all bacteria and many archaea, where it is the major cytoskeletal protein in the Z ring, required for cell division. Unlike some other cell organelles ... -
Turgor Pressure and Possible Constriction Mechanisms in Bacterial Division.
(Frontiers in microbiology, 2018-01-31)Bacterial cytokinesis begins with the assembly of FtsZ into a Z ring at the center of the cell. The Z-ring constriction in Gram-negative bacteria may occur in an environment where the periplasm and the cytoplasm are isoosmotic, ... -
Whole genome re-sequencing to identify suppressor mutations of mutant and foreign Escherichia coli FtsZ.
(PLoS One, 2017)FtsZ is an essential protein for bacterial cell division, where it forms the cytoskeletal scaffold and may generate the constriction force. We have found previously that some mutant and foreign FtsZ that do not complement ... -
ZipA and FtsA* stabilize FtsZ-GDP miniring structures.
(Sci Rep, 2017-06-16)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 ...
