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• W1588043867 abstract "After binding to its four 9-mer boxes in the 245-base pair Escherichia coli replication origin (oriC), dnaA protein effects the formation of an in an adjacent region made up of three 13-mers (Bramhill, D., and Kornberg, A. (1988) Cell 52, 743-755). This open complex formation requires the ATP form of dnaA protein assisted by HU protein (Sekimizu, K., Bramhill, D., and Kornberg, A. (1987) Cell 50, 259-265). We now provide direct evidence that dnaA protein binds the 13-mers, sequences that bear no resemblance to the 9-mer box. The evidence is (i) displacement of dnaA protein from the open complex by oriC or by a synthetic oligonucleotide containing the 13-mers, but not by a mutant of oriC lacking the 13-mers; (ii) filter binding of the synthetic (13-mer) oligonucleotide by dnaA protein; and (iii) requirement for the ATP form of dnaA protein assisted by HU protein for temperature-dependent binding to the 13-mer region. Controlled proteolysis of dnaA protein results in a prompt loss of oriC binding; an NH2-terminal 30-kDa peptide contains the domain that binds ATP and phospholipids known to destabilize the tightly bound ATP." @default.
• W1588043867 created "2016-06-24" @default.
• W1588043867 creator A5032237232 @default.
• W1588043867 creator A5074009134 @default.
• W1588043867 date "1989-04-01" @default.
• W1588043867 modified "2023-10-16" @default.
• W1588043867 title "The dnaA Initiator Protein Binds Separate Domains in the Replication Origin of Escherichia coli" @default.
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• W1588043867 doi "https://doi.org/10.1016/s0021-9258(18)83324-5" @default.
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