![]() pylori oriC exhibits bipartite structure, being the first such origin discovered in a Gram-negative bacterium. Surprisingly, oriC2 is bound exclusively as supercoiled DNA, which directly shows the importance of the DNA topology in DnaA- oriC interactions, similarly as previously presented only for initiator-origin interactions in Archaea and some Eukaryota. DnaA specifically binds both regions, but DnaA-dependent DNA unwinding occurs only within oriC2. ![]() Comprehensive in silico analysis presented in this work allowed us to identify an additional region ( oriC2), separated from the original one ( oriC1) by the dnaA gene. However, no unwinding within the oriC sequence has been detected. ![]() ![]() Helicobacter pylori oriC was previously identified as a region localized upstream of dnaA and containing a cluster of DnaA boxes bound by DnaA protein with a high affinity. Binding of the DnaA protein to oriC leads to DNA melting within the DNA unwinding element (DUE) and initiates replication of the bacterial chromosome. ![]()
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