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Volume 272, Number 1, Issue of January 3, 1997 pp. 83-88
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

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Occlusion of RNA Polymerase by Oligomerization of DnaA Protein over the dnaA Promoter of Escherichia coli

(Received for publication, June 25, 1996, and in revised form, September 13, 1996)

Yong Sun Lee ^§ and Deog Su Hwang

From the  Institute for Molecular Biology and Genetics and the ^§ Department of Microbiology, Seoul National University, Seoul 151-742, Korea

DnaA protein, the initiator protein for initiation of Escherichia coli chromosomal replication, has been shown to repress its own expression from two dnaA promoters, 1P and 2P. The sequence-specific binding of DnaA protein to the DnaA box, located between the two promoters, results in subsequent oligomerization of DnaA protein. Upon increasing the concentration of DnaA protein, the oligomerization proceeds to both dnaA promoters from the DnaA box and inhibits RNA polymerase binding to both promoters. This results in the repression of transcription, suggesting that the extent of oligomerization of DnaA proteins over two dnaA promoters contributes to the autoregulation of expression of the dnaA gene. When the two dnaA promoters were bound and repressed by DnaA protein, the interaction of RNA polymerase with IciA protein, which is a specific inhibitor of initiation of in vitro E. coli chromosomal replication, appeared to dissociate the oligomerized DnaA proteins from the 1P promoter and allowed RNA polymerase to be loaded for its transcription.

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