<p>Purified recombinant Dr-FtsZ and Ec-FtsZ were incubated in different combinations with GTP, ATP, Dr-FtsA (Dr) and Ec-FtsA (Ec) and the release of inorganic phosphate (Pi) was monitored (<b>A, B</b>). Similarly, Dr-FtsA (FtsA), Dr-FtsZ (FtsZ), ATP and [α 32P] GTP were incubated in different combinations and conversion of [α32P]-GTP substrate ([<sup>32</sup>P]α GTP) into [α32P] GDP product ([<sup>32</sup>P]α GDP) was monitored on TLC and autoradiogram was developed (<b>C</b>). Levels of both substrate (GTP) and product (GDP) were determined densitometrically for samples numbered as 1–6 as shown in panel C and plotted (<b>D</b>).</p
FtsZ polymerizes in a ring-like structure at mid cell to initiate cell division in Escherichia coli....
FtsZ, a tubulin homologue, forms a cytokinetic ring at the site of cell division in prokaryotes. The...
Introduction Nucleoside diphosphate kinase (NDK), conserved across bacteria to humans, synthesises N...
<p>Purified recombinant Dr-FtsZ (<b>A</b>) and Ec-FtsZ (<b>B</b>,) were incubated in different combi...
The Deinococcus radiodurans genome encodes homologues of divisome proteins including FtsZ and FtsA. ...
<p>Recombinant FtsZ and FtsA of <i>D. radiodurans</i> (Dr-FtsZ, Dr-FtsA) and <i>Escherichia coli</i>...
<p>Purified recombinant Dr-FtsA and Dr-FtsZ were incubated with GTP and [α32P]-ATP substrate in diff...
<p><b>A</b>. Purified recombinant Dr-FtsZ was incubated with increasing molar ratio of Dr-FtsA such ...
Factors contributing to the stability of bacterial cell division protein FtsZ remain unknown. In ord...
AbstractWe have analyzed the substrate kinetics of the GTPase activity of FtsZ and the effects of tw...
<p>Measured parameters for the GTPase activity and polymerization of FtsZ from <i>Escherichia coli</...
<p>Panel A, activity was determined indirectly by measuring a decrease in NADH concentration by its ...
Essential cell division protein FtsZ forms the bacterial cytokinetic ring and is a target for new an...
<p>Increasing concentration (1–10 µg) of Dr-FtsA and Ec-FtsA were incubated in the absence (<b>A</b>...
ABSTRACT Deinococcus radiodurans, a highly radioresistant bacterium, does not show LexA-dependent re...
FtsZ polymerizes in a ring-like structure at mid cell to initiate cell division in Escherichia coli....
FtsZ, a tubulin homologue, forms a cytokinetic ring at the site of cell division in prokaryotes. The...
Introduction Nucleoside diphosphate kinase (NDK), conserved across bacteria to humans, synthesises N...
<p>Purified recombinant Dr-FtsZ (<b>A</b>) and Ec-FtsZ (<b>B</b>,) were incubated in different combi...
The Deinococcus radiodurans genome encodes homologues of divisome proteins including FtsZ and FtsA. ...
<p>Recombinant FtsZ and FtsA of <i>D. radiodurans</i> (Dr-FtsZ, Dr-FtsA) and <i>Escherichia coli</i>...
<p>Purified recombinant Dr-FtsA and Dr-FtsZ were incubated with GTP and [α32P]-ATP substrate in diff...
<p><b>A</b>. Purified recombinant Dr-FtsZ was incubated with increasing molar ratio of Dr-FtsA such ...
Factors contributing to the stability of bacterial cell division protein FtsZ remain unknown. In ord...
AbstractWe have analyzed the substrate kinetics of the GTPase activity of FtsZ and the effects of tw...
<p>Measured parameters for the GTPase activity and polymerization of FtsZ from <i>Escherichia coli</...
<p>Panel A, activity was determined indirectly by measuring a decrease in NADH concentration by its ...
Essential cell division protein FtsZ forms the bacterial cytokinetic ring and is a target for new an...
<p>Increasing concentration (1–10 µg) of Dr-FtsA and Ec-FtsA were incubated in the absence (<b>A</b>...
ABSTRACT Deinococcus radiodurans, a highly radioresistant bacterium, does not show LexA-dependent re...
FtsZ polymerizes in a ring-like structure at mid cell to initiate cell division in Escherichia coli....
FtsZ, a tubulin homologue, forms a cytokinetic ring at the site of cell division in prokaryotes. The...
Introduction Nucleoside diphosphate kinase (NDK), conserved across bacteria to humans, synthesises N...