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A more recent version of this article appeared on September 7, 2001
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Papers In Press, published online ahead of print July 16, 2001
J. Biol. Chem, 10.1074/jbc.M101339200
Submitted on February 12, 2001
Revised on July 10, 2001
Accepted on July 13, 2001

SeqA protein aggregation is necessary for SeqA function

Ho Lee, Sukhyun Kang, Sung-Hun Bae, Byong-Seok Choi, and Deog Su Hwang

Institute of Molecular Biology and Genetics, Seoul National University, Seoul 151-742

Corresponding Author: dshwang{at}plaza.snu.ac.kr

The binding of SeqA protein to hemi-methylated GATC sequences is important in the negative modulation of chromosomal initiation at oriC, and in the formation of SeqA foci necessary for E. coli chromosome segregation. Using gel-filtration chromotography and glycerol gradient sedimentation, we demonstrate that SeqA exists as a homo-tetramer. 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 hemi-methylated DNA with altered binding patterns as compared to wild-type SeqA. Aggregates of SeqA(E9K) are defective in hemi-methylated DNA binding. Here we demonstrate that proper interaction between SeqA tetramers is required for both hemi-methylated 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.


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