Characterisation of recombinant FtsA of <i>Deinococcus radiodurans</i>.

<p>Recombinant FtsZ and FtsA of <i>D. radiodurans</i> (Dr-FtsZ, Dr-FtsA) and <i>Escherichia coli</i> (Ec-FtsZ, Ec-FtsA) were purified to homogeneity (<b>A</b>). Dr-FtsA was checked for typical secondary structure characteristics by Circular Dichroism in the absence (Control) and presence of 10 µM ATP (ATP) and in the presence of 8 M Urea (Urea) (<b>B</b>). [α32P]-ATP was incubated with recombinant DR1775 as a positive control (1) and in the absence (2) and presence (3) of Dr-FtsA and hydrolysis of [α32P]-ATP substrate ([³²P]α ATP) into [α32P]-ADP product ([³²P]α ADP) was monitored on Thin Layer Chromatography (TLC) and autoradiogram was developed as described in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0115918#s2" target="_blank">methods</a> (<b>C</b>). Effect of ATP on polymerization characteristic of Dr-FtsA (Con) was checked in the presence of Mg²⁺ (Mg) and Mg²⁺ + ATP (Mg+ATP) using transmission electron microscopy (<b>D</b>). Data shown in (<b>B</b>), (<b>C</b>) and (<b>D</b>) are the representative of the reproducible experiments repeated three times.