M.FokI methylates adenine in both strands of its asymmetric recognition sequence

D Landry; M C Looney; G R Feehery; B E Slatko; W E Jack; I Schildkraut; G G Wilson

doi:10.1016/0378-1119(89)90353-3

M.FokI methylates adenine in both strands of its asymmetric recognition sequence

Gene. 1989 Apr 15;77(1):1-10. doi: 10.1016/0378-1119(89)90353-3.

Authors

D Landry¹, M C Looney, G R Feehery, B E Slatko, W E Jack, I Schildkraut, G G Wilson

Affiliation

¹ New England Biolabs, Inc., Beverly, MA 01915.

PMID: 2744483
DOI: 10.1016/0378-1119(89)90353-3

Abstract

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.

MeSH terms

Adenine / metabolism*
Amino Acid Sequence
Chromatography, Thin Layer
DNA / metabolism
Flavobacterium / enzymology*
Flavobacterium / genetics
Methylation
Molecular Sequence Data
Oligodeoxyribonucleotides / chemical synthesis
Oligodeoxyribonucleotides / metabolism
Site-Specific DNA-Methyltransferase (Adenine-Specific) / isolation & purification
Site-Specific DNA-Methyltransferase (Adenine-Specific) / metabolism*
Substrate Specificity

Substances

Oligodeoxyribonucleotides
DNA
DNA modification methylase FokI
Site-Specific DNA-Methyltransferase (Adenine-Specific)
Adenine