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Nucleic Acids Research 2005 33(5):1524-1531; doi:10.1093/nar/gki289
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Published online 14 March 2005

© The Author 2005. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions{at}oupjournals.org

Article

Dimeric configuration of SeqA protein bound to a pair of hemi-methylated GATC sequences

Sukhyun Kang1, Joo Seok Han1, Keun Pill Kim1, Hye Yoon Yang1,2, Kyung Yong Lee1, Choo Bong Hong1,2 and Deog Su Hwang1,2,*

1Institute of Molecular Biology and Genetics, Seoul National University Seoul 151-742, Republic of Korea 2School of Biological Sciences, Seoul National University Seoul 151-742, Republic of Korea

*To whom correspondence should be addressed. Tel: +82 2 880 7524; Fax: +82 2 874 1206; Email: dshwang{at}plaza.snu.ac.kr

Received December 19, 2004. Revised February 18, 2005. Accepted February 18, 2005.

The binding of SeqA protein to hemi-methylated GATC sequences (hemi-sites) regulates chromosome initiation and the segregation of replicated chromosome in Escherichia coli. We have used atomic force microscopy to examine the architecture of SeqA and the mode of binding of one molecule of SeqA to a pair of hemi-sites in aqueous solution. SeqA has a bipartite structure composed of a large and a small lobe. Upon binding of a SeqA molecule to a pair of hemi-sites, the larger lobe becomes visibly separated into two DNA binding domains, each of which binds to one hemi-site. The two DNA binding domains are held together by association between the two multimerization domains that make up the smaller lobe. The binding of each DNA binding domain to a hemi-site leads to bending of the bound DNA inwards toward the bound protein. In this way, SeqA adopts a dimeric configuration when bound to a pair of hemi-sites. Mutational analysis of the multimerization domain indicates that, in addition to multimerization of SeqA polypeptides, this domain contributes to the ability of SeqA to bind to a pair of hemi-sites and to its cooperative behavior.

The authors wish it to be known that, in their opinion, the first three authors should be regarded as joint First Authors


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