Open AccessCloning and sequence analysis of the Stsl restriction-modification gene: presence of homology to Fokl restriction-modification enzymes
Author(s) -
Keiko Kita,
Masaaki Suisha,
Hirokazu Kotani,
Hideshi Yanase,
Nobuo Kato
Publication year - 1992
Publication title -
nucleic acids research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 9.008
H-Index - 537
eISSN - 1362-4954
pISSN - 0305-1048
DOI - 10.1093/nar/20.16.4167
Subject(s) - biology , restriction enzyme , foki , endonuclease , nucleic acid sequence , gene , genetics , microbiology and biotechnology , peptide sequence , homology (biology) , recognition sequence , sequence analysis , amino acid , dna , biochemistry , allele , polymorphism (computer science)
StsI endonuclease (R.StsI), a type IIs restriction endonuclease found in Streptococcus sanguis 54, recognizes the same sequence as FokI but cleaves at different positions. A DNA fragment that carried the genes for R.StsI and StsI methylase (M.StsI) was cloned from the chromosomal DNA of S.sanguis 54, and its nucleotide sequence was analyzed. The endonuclease gene was 1,806 bp long, corresponding to a protein of 602 amino acid residues (M(r) = 68,388), and the methylase gene was 1,959 bp long, corresponding to a protein of 653 amino acid residues (M(r) = 76,064). The assignment of the endonuclease gene was confirmed by analysis of the N-terminal amino acid sequence. Genes for the two proteins were in a tail-to-tail orientation, separated by a 131-nucleotide intercistronic region. The predicted amino acid sequences between the StsI system and the FokI system showed a 49% identity between the methylases and a 30% identity between the endonucleases. The sequence comparison of M.StsI with various methylases showed that the N-terminal half of M.StsI matches M.NIaIII, and the C-terminal half matches adenine methylases that recognize GATC and GATATC.