[A new site specific endonuclease-methylase from a thermophilic strain of Bacillus species LU11].
A new site-specific endonuclease BspLU11III was purified to homogeneity from a thermophilic strain Bacillus species LU11. BspLU11III recognizes the 5'-GGGAC-3' sequence on the double-stranded DNA and cleaves the 10/14 and 11/15 nucleotides in different strands away from the recognition site. The enzyme exists in solution as a monomer with a molecular mass of about 93 kDa. When incubated with S-adenosyl-L-methionine, BspLU11III displays a DNA-methyltransferase activity. The adenine residue is methylated inside the recognition site 5'-GGGAC-3' in the only strand. The restriction activity does not change in the presence of ATP but is stimulated by 80 microM S-adenosyl-L-methionine (4-fold). Magnesium cations are needed for the restriction activity. Sodium chloride stimulates the "star" activity of BspLU11III. According to its properties, BspLU11III can be classified as a type IV endonuclease.
Chernov
A V
AV
Matvienko
N N
NN
Zheleznaia
L A
LA
Matvienko
N I
NI
D001407:Bacillus / Q000201:enzymology*; D001483:Base Sequence; D002850:Chromatography, Gel; D004247:DNA / Q000378:metabolism; D015280:DNA Restriction-Modification Enzymes / Q000302:isolation & purification / Q000378:metabolism*; D004587:Electrophoresis, Agar Gel; D008969:Molecular Sequence Data; D008970:Molecular Weight; D013379:Substrate Specificity
D015280:DNA Restriction-Modification Enzymes; D004247:DNA; C092321:endodeoxyribonuclease BspLU11III
Novaia saĭt-spetsificheskaia éndonukleaza-metilaza iz termofil'nogo shtamma Bacillus species LU11.