<p>A. Representative light scattering trace of an experiment performed with wild-type FtsZ in the absence of inhibitor and in the presence of MinC or MinC19. Reactions contained 7 µM of FtsZ and 20 µM of MinC or MinC19 in Mes/NaOH 50 mM, MgCl<sub>2</sub> 10 mM, KCl 133 mM, DEAE-dextran 0.6 mg/mL, pH 6.5. B. Experiments similar to A were performed and the inhibition of the polymerization of each FtsZ mutant by MinC was quantified relative to the maximum light scattering signal in the absence of MinC. The original light scattering traces corresponding to this graph can be found in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0060690#pone.0060690.s004" target="_blank">Fig. S4</a>. Measurements were repeated at least th...
<p>A. Purified MBP-ABDOM bound assembled FtsZ <i>in vitro</i>. The MBP-ABDOM fusion protein, but not...
During bacterial cell division, the essential protein FtsZ assembles in the middle of the cell to fo...
Background: Cell division in Bacillus subtilis occurs precisely at midcell. Positional control of ce...
<p>A) Polymerization of FtsZ with or without the addition of SlmA and SBS17-30mer. Reactions were pe...
<p>(A) Rates of GTP hydrolysis were measured in reactions containing FtsZ wild type or mutant (5 µM)...
<p>A. MinC was included in degradation reactions containing FtsZ with GTP and ClpXP (0.5 µM). B. Fts...
<p>(A) Cells with <i>ftsZ<sub>V208A</sub></i> or <i>ftsZ<sub>L169R</sub></i> form FtsZ rings and do ...
<p>Wild-type or double-mutant (K243R,D287V) FtsZ <b>(</b>2 µM) were mixed with 1 µM MinC Y44W in buf...
The min system prevents polar cell division in bacteria. Here, the biochemical characterization of t...
<p>Purified wild-type and mutant FtsZ were polymerized in reactions containing 5 µM of FtsZ, Mes/NaO...
AbstractThe min system prevents polar cell division in bacteria. Here, the biochemical characterizat...
During bacterial cell division, the essential protein FtsZ assembles in the middle of the cell to fo...
Cell division in bacteria is regulated by proteins that interact with FtsZ and modulate its ability ...
<p>FtsZ monomers are depicted as having one nucleotide molecule, either GDP or GTP. Polymers form on...
Cell division in bacteria is regulated by proteins that interact with FtsZ and modulate its ability ...
<p>A. Purified MBP-ABDOM bound assembled FtsZ <i>in vitro</i>. The MBP-ABDOM fusion protein, but not...
During bacterial cell division, the essential protein FtsZ assembles in the middle of the cell to fo...
Background: Cell division in Bacillus subtilis occurs precisely at midcell. Positional control of ce...
<p>A) Polymerization of FtsZ with or without the addition of SlmA and SBS17-30mer. Reactions were pe...
<p>(A) Rates of GTP hydrolysis were measured in reactions containing FtsZ wild type or mutant (5 µM)...
<p>A. MinC was included in degradation reactions containing FtsZ with GTP and ClpXP (0.5 µM). B. Fts...
<p>(A) Cells with <i>ftsZ<sub>V208A</sub></i> or <i>ftsZ<sub>L169R</sub></i> form FtsZ rings and do ...
<p>Wild-type or double-mutant (K243R,D287V) FtsZ <b>(</b>2 µM) were mixed with 1 µM MinC Y44W in buf...
The min system prevents polar cell division in bacteria. Here, the biochemical characterization of t...
<p>Purified wild-type and mutant FtsZ were polymerized in reactions containing 5 µM of FtsZ, Mes/NaO...
AbstractThe min system prevents polar cell division in bacteria. Here, the biochemical characterizat...
During bacterial cell division, the essential protein FtsZ assembles in the middle of the cell to fo...
Cell division in bacteria is regulated by proteins that interact with FtsZ and modulate its ability ...
<p>FtsZ monomers are depicted as having one nucleotide molecule, either GDP or GTP. Polymers form on...
Cell division in bacteria is regulated by proteins that interact with FtsZ and modulate its ability ...
<p>A. Purified MBP-ABDOM bound assembled FtsZ <i>in vitro</i>. The MBP-ABDOM fusion protein, but not...
During bacterial cell division, the essential protein FtsZ assembles in the middle of the cell to fo...
Background: Cell division in Bacillus subtilis occurs precisely at midcell. Positional control of ce...