Nucleic Acids Research, 1989, Vol. 17, No. 7 2421-2435
© 1989
MOLECULAR BIOLOGY |
Predictive motifs derived from cytosine methyltransferases
Cold Spring Harbor Laboratory PO Box 100, Cold Spring Harbor, NY 11724, USA +Permanent addresses: Institute of Biophysics, Biological Research Centre, Hungarian Academy of Sciences Szeged, PO Box 521, 6701 Hungary *Present addresses: Wayne State University 435 Chemistry, Detroit, MI 48202, USA 1University of Wisconsin, McArdle Laboratory for Cancer Research 450 N-Randall Avenue, Madison, WI 53705, USA øPermanent addresses: Institute of Biochemistry, Biological Research Centre, Hungarian Academy of Sciences Szeged, PO Box 521, 6701 Hungary
Received January 19, 1989. Accepted February 23, 1989.
Thirteen bacterial DNA methyltransferases that catalyze the formation of 5-methylcytosine within specific DNA sequences possess related structures. Similar building blocks (motifs), containing invariant positions, can be found in the same order in all thirteen sequences. Five of these blocks are highly conserved while a further five contain weaker similarities. One block, which has the most invariant residues, contains the proline-cysteine dipeptide of the proposed catalytic site. A region in the second half of each sequence is unusually variable both in length and sequence composition. Those methyltransferases that exhibit significant homology in this region share common specificity in DNA recognition. The five highly conserved motifs can be used to discriminate the known 5-methylcytosine forming methyltransferases from all other methyltransferases of known sequence, and from all other identified proteins in the PIR, GenBank and EMBL databases. These five motifs occur in a mammalian methyltransferase responsible for the formation of 5-methylcytosine within CG dinucleotides. By searching the unidentified open reading frames present in the GenBank and EMBL databases, two potential 5-methylcytosine forming methyltransferases have been found.
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