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Nucleic Acids Research, 1991, Vol. 19, No. 5 1049-1056
© 1991

ENZYMOLOGY

Stepwise cloning and molecular characterization of the HgiDI restriction-modification system from Herpetosiphon giganteus Hpa2

Andreas Düsterhäft, Dirk Erdmann and Manfred Kröger*

Institut für Mikrobiologie und Molekularbiologie der Justus-Liebig-Universität Giessen FB 15 Frankfurter Strasse 107, D-6300 Giessen, FAG

* To whom correspondence should be addressed

Received December 10, 1990. Revised January 28, 1991. Accepted January 28, 1991.

The restriction-modification system H9iDl from Herpetosiphon giganteus strain Hpa2 has been cloned in E. coil in a two-step procedure. Selection of the methyltransferase (M.HglDl)gene in vitro was performed using the heterolgous restriction endonuciease Ahall, an Isoschlzomer of Acyl and HglDl (GRCGYC). Cloning of the complete HglDl endonuclease (R.H9lDl) gene could only be achieved in recipient cells harbouring a recombinant plasmid, which was expressing the corresponding methyitransterase and could thereby prevent the host from self-destruction of its genetic material. The HglDl restriction-modification system was sequenced and functionally correlated with two open reading frames of 309 (M) and 359 (R) codons. In homology studies M.HglDl showed significant similarities to 20 other m5C-methytrases and turned out to be the most compact enzyme of this group described so far. Initial attempts for overexpression of M.HglDl and partial purification of R.HglDl have been successful.


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