M.FokI methylates adenine in both strands of its asymmetric recognition sequence.
M.FokI, a type-IIS modification enzyme from Flavobacterium okeanokoites, was purified, and its activity was characterized in vitro. The enzyme was found to be a DNA-adenine methyltransferase and to methylate both strands of the asymmetric FokI recognition sequence: (formula; see text) M.FokI does not methylate single-stranded DNA, nor does it methylate double-stranded DNA at sequences other than FokI sites.
Landry
D
D
New England Biolabs, Inc., Beverly, MA 01915.
Looney
M C
MC
Feehery
G R
GR
Slatko
B E
BE
Jack
W E
WE
Schildkraut
I
I
Wilson
G G
GG
D000225:Adenine / Q000378:metabolism*; D000595:Amino Acid Sequence; D002855:Chromatography, Thin Layer; D004247:DNA / Q000378:metabolism; D005417:Flavobacterium / Q000201:enzymology* / Q000235:genetics; D008745:Methylation; D008969:Molecular Sequence Data; D009838:Oligodeoxyribonucleotides / Q000138:chemical synthesis / Q000378:metabolism; D015265:Site-Specific DNA-Methyltransferase (Adenine-Specific) / Q000302:isolation & purification / Q000378:metabolism*; D013379:Substrate Specificity
D009838:Oligodeoxyribonucleotides; D004247:DNA; C058668:DNA modification methylase FokI; D015265:Site-Specific DNA-Methyltransferase (Adenine-Specific); D000225:Adenine