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J. Biol. Chem., Vol. 276, Issue 37, 34600-34606, September 14, 2001
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From the The binding of SeqA protein to hemimethylated
GATC sequences is important in the negative modulation of chromosomal
initiation at oriC, and in the formation of SeqA foci
necessary for Escherichia coli chromosome segregation.
Using gel-filtration chromotography and glycerol gradient
sedimentation, we demonstrate that SeqA exists as a homotetramer. SeqA
tetramers are able to aggregate or multimerize in a reversible,
concentration-dependent manner. Using a bacterial two-hybrid
system, we demonstrate that the N-terminal region of SeqA,
especifically the 9th amino acid residue, glutamic acid, is required
for functional SeqA-SeqA interaction. Although the SeqA(E9K) mutant
protein, containing lysine rather than glutamic acid at the 9th amino
acid residue, exists as a tetramer, the mutant protein binds to
hemimethylated DNA with altered binding patterns as compared with
wild-type SeqA. Aggregates of SeqA(E9K) are defective in hemimethylated
DNA binding. Here we demonstrate that proper interaction between SeqA
tetramers is required for both hemimethylated DNA binding and formation
of active aggregates. SeqA tetramers and aggregates might be involved
in the formation of SeqA foci required for the segregation of
chromosomal DNA as well as the regulation of chromosomal initiation.
Institute of Molecular Biology and Genetics,
School of Biological Sciences, Seoul National University, Seoul
151-742, Korea and the Department of Chemistry and National
Creative Research Initiative Center, Korea Advanced Institute of
Science and Technology, Taejon 305-701, Korea
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J. S. Han, S. Kang, H. Lee, H. K. Kim, and D. S. Hwang Sequential Binding of SeqA to Paired Hemi-methylated GATC Sequences Mediates Formation of Higher Order Complexes J. Biol. Chem., September 12, 2003; 278(37): 34983 - 34989. [Abstract] [Full Text] [PDF]
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