The dnaA initiator protein binds separate domains in the replication origin of Escherichia coli

B. Y. Yung, A. Kornberg

研究成果: 期刊稿件文章同行評審

75 引文 斯高帕斯(Scopus)

摘要

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 'open complex' 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 proteins 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.

原文英語
頁(從 - 到)6146-6150
頁數5
期刊Journal of Biological Chemistry
264
發行號11
出版狀態已出版 - 1989
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