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- W2009491206 abstract "In Escherichia coli, the replication origin oriC consists of two functional regions: the duplex unwinding element (DUE) and its flanking DnaA-assembly region (DAR). ATP-DnaA molecules multimerize on DAR, unwinding DUE for DnaB helicase loading. However, DUE-unwinding mechanisms and functional structures in DnaA-oriC complexes supporting those remain unclear. Here, using various in vitro reconstituted systems, we identify functionally distinct DnaA sub-complexes formed on DAR and reveal novel mechanisms in DUE unwinding. The DUE-flanking left-half DAR carrying high-affinity DnaA box R1 and the ATP-DnaA-preferential DnaA box R5, τ1-2 and I1-2 sites formed a DnaA sub-complex competent in DUE unwinding and ssDUE binding, thereby supporting basal DnaB loading activity. This sub-complex is further subdivided into two; the DUE-distal DnaA sub-complex formed on the ATP-DnaA-preferential sites binds ssDUE. Notably, the DUE-flanking, DnaA box R1-DnaA sub-complex recruits DUE to the DUE-distal DnaA sub-complex in concert with a DNA-bending nucleoid protein IHF, thereby promoting DUE unwinding and binding of ssDUE. The right-half DAR-DnaA sub-complex stimulated DnaB loading, consistent with in vivo analyses. Similar features are seen in DUE unwinding of the hyperthermophile, Thermotoga maritima, indicating evolutional conservation of those mechanisms." @default.
- W2009491206 created "2016-06-24" @default.
- W2009491206 creator A5061099628 @default.
- W2009491206 creator A5074227066 @default.
- W2009491206 date "2011-11-02" @default.
- W2009491206 modified "2023-09-30" @default.
- W2009491206 title "Highly organized DnaA– oriC complexes recruit the single-stranded DNA for replication initiation" @default.
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- W2009491206 doi "https://doi.org/10.1093/nar/gkr832" @default.
- W2009491206 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3287180" @default.
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