DNase I footprints of Eσ in the presence or absence of CRP and CRP on CC-50

Abstract

<p><b>Copyright information:</b></p><p>Taken from "Interplay between CRP-cAMP and PII-Ntr systems forms novel regulatory network between carbon metabolism and nitrogen assimilation in "</p><p></p><p>Nucleic Acids Research 2007;35(5):1432-1440.</p><p>Published online 6 Feb 2007</p><p>PMCID:PMC1865078.</p><p>© 2007 The Author(s).</p>5 (A CRP consensus-binding site was introduced into position −50.5 nucleotides upstream of the p2) or wild-type p2. CRP, CRP and Eσ, when added, were present at a final concentration of 50 nM. Lanes 1 and 8 are A+G marker ladders. The limits of protected regions are indicated. On p2, only wild-type CRP can bind co-operatively with Eσ and the protection region is comparable to the one on CC-50.5. The locations of specific protected or hypersensitive bands are different on the two templates due to the difference of the sequence of CRP-binding sites. The hypersensitive band due to the CRP-binding on p2 is marked by arrow. The protection of αCTD binding, which is co-operative only with wild-type CRP, is similar on both p2 and CC-50.5 (lanes 5 and 12). These results strongly support that the relative orientation between CRP and Eσ is similar on p2 and CC-50.5