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Nucleic Acids Research, 1991, Vol. 19, No. 18 4843-4847
© 1991

MOLECULAR BIOLOGY

Complementation by detached parts of GGCC-specific DNA methyltransferases

György Pósfai, Sun C. Kim1, László Szilák, Attila Kovács and Pál Venetianer

Institute of Biochemistry, Biological Research Center of the Hungarian Academy of Sciences PO Box 521, 6701 Szeged, Hungary 1McArdle Laboratory for Cancer Research, University of Wisconsin Madison, WI 53706, USA

Received July 19, 1991. Accepted August 19, 1991.

Individually inactive N- and C-terminal fragments of the m5C-methyltransferase M.flspRI can complement each other resulting in specific, in vivo methylatlon of the DNA. This was shown by cloning the coding regions for N- and C-terminal parts of the enzyme in compatible plasmids and co-transforming them into E.coli cells. The enzyme could be detached at several different sites, producing either non-overlapping or partially overlapping fragments capable of complementation. Reconstitution of the active methyltransferase from inactive fragments was demonstrated in vitro, as well. Another GGCC-specific methyltransferase, M.BsuRI, showed a similar complementation phenomenon. Moreover, interspecles complementation was observed between appropriate fragments of the two closely related enzymes M.BspRI and M.BsuRI. Fragments of structurally and functionally more different methyltransferases were unable to complement each other.


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