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Journal of Bacteriology, October 2005, p. 6998-7008, Vol. 187, No. 20
0021-9193/05/$08.00+0 doi:10.1128/JB.187.20.6998-7008.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.
Sung-Hun Bae,3,
Sang Hoon Yun,1,
Hee Jung Lee,1
Sang Chun Ji,1
Ji Hyun Lee,1
Preeti Srivastava,2
Seol-Hoon Lee,3
Huiseok Chae,3
Younghoon Lee,3
Byong-Seok Choi,3
Dhruba K. Chattoraj,2 and
Heon M. Lim1*
Department of Biology, School of Biological Sciences and Biotechnology, Chungnam National University, Taejon, 305-764 Korea,1 Laboratory of Biochemistry, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892-4255,2 Department of Chemistry, Korea Advanced Institute of Science and Technology, Taejon, 305-701, Korea3
Received 29 April 2005/ Accepted 1 August 2005
We have found, using a newly developed genetic method, a protein (named Cnu, for oriC-binding nucleoid-associated) that binds to a specific 26-base-pair sequence (named cnb) in the origin of replication of Escherichia coli, oriC. Cnu is composed of 71 amino acids (8.4 kDa) and shows extensive amino acid identity to a group of proteins belonging to the Hha/YmoA family. Cnu was previously discovered as a protein that, like Hha, complexes with H-NS in vitro. Our in vivo and in vitro assays confirm the results and further suggest that the complex formation with H-NS is involved in Cnu/Hha binding to cnb. Unlike the hns mutants, elimination of either the cnu or hha gene did not disturb the growth rate, origin content, and synchrony of DNA replication initiation of the mutants compared to the wild-type cells. However, the cnu hha double mutant was moderately reduced in origin content. The Cnu/Hha complex with H-NS thus could play a role in optimal activity of oriC.
M.S.K., S.-H.B., and S.H.Y. contributed equally to this work.
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