[Isolation, purification and properties of restrictase and methylase BstN1 from Bacillus stearothermophilus].
Restriction-methylation enzymes BstN1 from Bacillus stearothermophilus were isolated and purified. These enzymes are related to a new class of restriction-methylation enzymes of the second type, whose modifying component is N4-cytosine-DNA-methylase. Both enzymes recognize the DNA sequence CC(A/T)GG. Restrictase BstN1 is a protein made up of one subunit with a molecular mass of 25 kDa. The molecular mass of native DNA-methylase BstN1 is about 55 kDa. The temperature optima for restrictase and methylase BstN1 are around 60 degrees C. Possible uses of BstN1 restriction-methylation enzymes for the analysis of cytosine methylation in bacterial and higher plant DNA are discussed.
Baryshev
M M
MM
Bur'ianov
Ia I
IaI
Kosykh
V G
VG
Baev
A A
AA
D001483:Base Sequence; D002848:Chromatography, DEAE-Cellulose; D004247:DNA / Q000378:metabolism; D015257:DNA-Cytosine Methylases / Q000302:isolation & purification* / Q000378:metabolism; D015252:Deoxyribonucleases, Type II Site-Specific / Q000302:isolation & purification* / Q000378:metabolism; D004587:Electrophoresis, Agar Gel; D001411:Geobacillus stearothermophilus / Q000201:enzymology*; D008745:Methylation; D008970:Molecular Weight; D013379:Substrate Specificity
D004247:DNA; C029528:DNA modification methylase EcoRII; D015257:DNA-Cytosine Methylases; C046545:CCWGG-specific type II deoxyribonucleases; D015252:Deoxyribonucleases, Type II Site-Specific
Vydelenie, ochistka i nekotorye svoĭstva restriktazy i metilazy BstN1 iz Bacillus stearothermophilus.