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Nucleic Acids Research, 1992, Vol. 20, No. 4 705-709
© 1992

ENZYMOLOGY

Cloning and expression of the Hpal restriction-modification genes

Hiroyuki Ito, Harumi Shimato, Atsuko Sadaok, Hirokazu Kotani, Fusao Kimizuka and Ikunoshin Kato1

Bioproducts Development Center, Takara Shuzo Co., Ltd Seta 3-4-1, Otsu, Shiga 520-21, Japan 1Biotechnology Research Laboratories, Takara Shuzo Co., Ltd Seta 3-4-1, Otsu, Shiga 520-21, Japan

Received December 5, 1991. Revised January 28, 1992. Accepted January 28, 1992.

The genes from Haemophilus parainfiuenzae encoding the Hpal restriction-modification system were cloned and expressed in Escherichia coli. From the DNA sequence, we predicted the Hpal endonuclease (R-Hpal) to have 254 amino acid residues (Mr 29,630) and the Hpal methyltransferase (M-Hpal) to have 314 amino acid residues (37,390). The R. Hpal and M-Hpal genes overlapped by 16 base pairs on the chromosomal DNA. The genes had the same orientation. The clone, named E. coli HB101-HPA2, overproduced R-Hpal. R-Hpal activity from the clone was 100-fold that from H. parainfluenzae. The amino acid sequence of M -Hpal was compared with those of other type II methyltransferases.


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