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Nucleic Acids Research, 1990, Vol. 18, No. 13 3903-3911
© 1990

MOLECULAR BIOLOGY

Cloning, nucleotide sequence, and expression of the Hincll restriction-modification system

Hiroyuki Ito, Atsuko Sadaoka, Hirokazu Kotani, Nobutsugu Hiraoka and Teruya Nakamura

Bioproducts Development Center Takara Shuzo Co., Ltd., Seta 3–4–1, Otsu, Shiga 520–21, Japan

Received March 9, 1990. Revised May 30, 1990. Accepted May 30, 1990.

Two genes, coding for the Hincll from Haemophilus influenzae Re restriction-modification system, were cloned and expressed in Escherichia coli RR1. Their DNA sequences were determined. The Hincll methylase (M.Hincll) gene was 1, 506 base pairs (bp) long, corresponding to a protein of 502 amino acid residues (Mr=55, 330). The Hincll endonuclease (R.Hincll) gene was 774 bp long, corresponding to a protein of 258 amino acid residues (Mr = 28, 490). The amino acid residues predicted from the R.Hincll and the N-terminal amino acid sequence of the enzyme found by analysis were identical. These methylase and endonuclease genes overlapped by 1 bp on the H. infiuenzae Re chromosomal DNA. The clone, named E. coli RR1-Hincll, overproduced R.Hincll. The R.Hincll activity of this clone was 1, 000-fold that from H. influenzae Rc. The amino acid sequence of M.Hincll was compared with the sequences of four other adenine-specific type II methylases. Important homology was found between the M.Hincll and these other methylases.


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