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Papers In Press, published online ahead of print May 18, 2004
Institute of Molecular Biology and Genetics, School of Biological Sciences, Seoul National University, Seoul 151-742
Corresponding Author: dshwang{at}plaza.snu.ac.kr
SeqA protein regulates chromosome initiation and is involved in segregation in E. coli. One SeqA protein binds to two hemi-methylated GATC sequences to form a stable SeqA-DNA complex. We found that binding induced DNA bending which was pronounced when the two sequences were on the same face of the DNA. Two SeqA molecules bound cooperatively to each pair of hemi-methylated sites when the spacing between the sites was 30 bp. This cooperative binding was able to stabilize the binding of a wild type to a single hemi-methylated site or mutant form of SeqA protein to hemi-methylated sites, whereas such binding did not occur without the cooperative interaction. Two cooperatively bound SeqA molecules interacted with another SeqA bound up to 185 bp away from the two bound SeqA and this was followed by aggregation of free SeqA proteins onto the bound proteins. These results suggest that the step-wise interaction of SeqA proteins with hemi-methylated GATC sites enhances their interaction and leads to the formation of SeqA aggregates. Cooperative interaction followed by aggregation may be the driving force for formation of the SeqA foci that appear to be located behind replication forks.
J. Biol. Chem, 10.1074/jbc.M402612200
Submitted on March 8, 2004
Revised on May 14, 2004
Accepted on May 18, 2004
Binding of SeqA protein to hemi-methylated GATC sequences enhances their interaction and aggregation properties
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