Chromatography A Ccda Ccdb 1 1 Mixture A 85 Bp Dna Fragment Mh12

Chromatography A Ccda Ccdb 1 1 Mixture A 85 Bp Dn A ccda:ccdb 1:1 mixture, a 85 bp dna fragment mh12, and the ccda:ccdb 1:1 and 1:2 mixtures with this 85 bp dna fragment analyzed on an analytical gel filtration column are shown. inset , c4 reverse phase chromatographic profile at 280 nm of the gel filtration peak ( red ) of the ccda:ccdb 1:1 dna mixture. A ccda: ccdb 1:1 mixture, a 85 bp dna fragment mh12, and the ccda:ccdb 1:1 and 1:2 mixtures with this 85 bp dna fragment analyzed on an analytical gel filtration column are shown.

Chromatography A Ccda Ccdb 1 1 Mixture A 85 Bp Dn , binding of ccda (2.5 μm) and of equimolar concentrations of ccda and ccdb (2.5 μm) to the f4r1 fragment (lower strand labeled). c, dna sequence of the control region of the . ccd. operon. sequences corresponding to the f4 and r1 oligonucleotides are . underlined; regions corresponding to the op12, pal, prom and mh12 fragments are indicated by. Separate the bseri digested p15a ampccdb plasmid fragment using agarose gel electrophoresis, running the gel at a field strength of 4 v cm −1 for 1 h and purify the dna fragment using the. The ccd toxin antitoxin system is involved in plasmid maintenance and bacterial persistence. the ccda antitoxin accelerates dissociation of ccdb from its complex with dna gyrase, binds and neutralizes ccdb, but the mechanistic details are unclear. using a series of experimental and computational approaches, we demonstrate the formation of. The persistence of free o p independently of the amount of ccdb suggests that ccda is the limiting factor for binding of the ccda–ccdb complex. as the ccdb concentration increased further (0.8–1.6 µm), the amount of mobility shifted complexes decreased sharply, and free o p was released (fig. 2a). figure 2.