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Nucleic Acids Research, 1991, Vol. 19, No. 23 6505-6509
© 1991

MOLECULAR BIOLOGY

Genetic organization of the KpnI restriction — modification system

Deb K. Chatterjee, Alan W. Hammond, Robert W. Blakesley, Shelia M. Adams and Gary F. Gerard

Life Technologies, Inc. 8717 Grovemont Circle, Gaithersburg, MD 20877, USA

Received August 14, 1991. Accepted October 31, 1991.

The KpnI restriction-modification (KpnI RM) system was previously cloned and expressed in E. coli. The nucleotide sequences of the Kpnl endonuclease (R. KpnI) and methylase (M. KpnI) genes have now been determined. The sequence of the amino acid residues predicted from the endonuclease gene DNA sequence and the sequence of the first 12 NH2-terminal amino acids determined from the purified endonuclease protein were identical. The kpnIR gene specifies a protein of 218 amino acids (MW: 25,115), while the kpnIM gene codes for a protein of 417 amino acids (MW: 47,582). The two genes transcribe divergently with a intergenenic region of 167 nucleotides containing the putative promoter regions for both genes. No protein sequence similarity was detected between R. KpnI and M. KpnI. Comparison of the amino acid sequence of M.KpnI with sequences of various methylases revealed a significant homology to N6-adenine methylases, a partial homology to N4-cytosine methylases, and no homology to C5-methylases.


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S. Bheemanaik, S. Chandrashekaran, V. Nagaraja, and D. N. Rao
Kinetic and Catalytic Properties of Dimeric KpnI DNA Methyltransferase
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