Open AccessIsolation and characterization of a type II restriction endonuclease from Streptococcus thermophilus
Author(s) -
Solaiman Daniel K.Y.,
Somkuti George A.
Publication year - 1990
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1990.tb04030.x
Subject(s) - isoschizomer , restriction enzyme , hpaii , endonuclease , streptococcus thermophilus , ligation , biology , microbiology and biotechnology , dna , chemistry , biochemistry , genetics , bacteria , gene , gene expression , dna methylation , lactobacillus
A type II restriction endonuclease Sth 1341 was isolated from Streptococcus thermophilus strain 134. The enzyme is an isoschizomer of Hpa II. The restriction endonuclease is most active at Mg(II) ?5 mM; in the pH range of 7.5–8; temperature of 50°–55°C; and (KCl) or (NaCl) below 100 mM. Double digestion and ligation experiments showed that Sth 1341 apparently recognized and cleaves DNA at the sequence C 1 CGG to produce two‐base, 5′‐protruding ends.