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- W2075067980 abstract "DnaA protein binds to the chromosomal origin (oriC) to initiate DNA replication. We developed an efficient system for purification of DnaA protein which will facilitate physicochemical analysis of the protein. The yield of DnaA protein was increased at least 6-fold compared to an available method being used, and over 22 mg of the protein were obtained from only 100 g of cells. DnaA protein purified by this procedure showed an indistinguishable affinity for ATP, and activity forin vitroreplication oforiCplasmid. The process of denaturation of DnaA protein, which was blocked by ATP, was monitored by intrinsic fluorescence and circular dichroism. Analysis of circular dichroism revealed that DnaA protein is rich in α-helices, and that ATP-binding leads to a significant transition of protein conformation in that the content of α-helices is decreased. This is the first evidence indicating that ATP-binding profoundly affects conformation of DnaA protein." @default.
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- W2075067980 date "1997-03-01" @default.
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- W2075067980 title "Conformational Transition of DnaA Protein by ATP: Structural Analysis of DnaA Protein, the Initiator ofEscherichia coliChromosome Replication" @default.
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- W2075067980 doi "https://doi.org/10.1006/bbrc.1997.6244" @default.
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