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Nucleic Acids Research, 1991, Vol. 19, No. 5 1007-1013
© 1991

MOLECULAR BIOLOGY

Cloning and characterization of the Mboll restriction-modification system

Hubertus Bocklage, Karin Heeger and Benno Müller-Hill*

Institut für Genetik der Universität zu Köln Weyertal 121, 5000 Köln 41, FRG

* To whom correspondence should be addressed

Received January 4, 1991. Revised February 8, 1991. Accepted February 8, 1991.

The two genes encoding the class llS restriction-modification system Mboll from Moraxella bovis were cloned separately in two compatible plasmids and expressed in E. coll RR1{Delta}M15. The nucleotide sequences of the Mboll endonuclease (R.Mboll) and methylase (M.Mboll) genes were determined and the putative start codon of R.Mboll was confirmed by amino acid sequence analysis. The mbollR gene specifies a protein of 416 amino acids (MW: 48,617) while the mbollM gene codes for a putative 260-residue polypeptlde (MW: 30,077). Both genes are aligned in the same orientation. The coding region of the methylase gene ends 11 bp upstream of the start codon of the restrictase gene. Comparing the amino acid sequence of M.Mboll with sequences of other N6-adenine methyltransterases reveals a significant homology to M.Rsrl, M.Hlnfl and M.DpnA. Furthermore, M.Mboll shows homology to the N4-cytosine methyltransferase BamHl.


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