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

Gene ·Vol. 77 ·No. 1 ·1989-04-15 ·Pages 1-10

Landry D, Looney MC, Feehery GR, Slatko BE, Jack WE, Schildkraut I, Wilson GG

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,genetics Methylation Molecular Sequence Data Oligodeoxyribonucleotides/chemical synthesis,metabolism Site-Specific DNA-Methyltransferase (Adenine-Specific)/isolation & purification,metabolism Substrate Specificity

Chemicals

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

Authors & Affiliations

7 authors, click to expand affiliations / ORCID

Landry D

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

Looney M C

Feehery G R

Slatko B E

Jack W E

Schildkraut I

Wilson G G

Article Info

Journal

Gene

Abbr.

Gene

ISSN

0378-1119

DOI

10.1016/0378-1119(89)90353-3

Published

1989-04-15

Pages

1-10

Language

English

Region

Netherlands

NLM ID

7706761

Subset

External Links

PubMed source DOI: 10.1016/0378-1119(89)90353-3 View journal details

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

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