M · FokI methylates adenine in both strands of its asymmetric recognition sequence
| Autor: | David Landry, Ira Schildkraut, William E. Jack, Geoffrey G. Wilson, Barton E. Slatko, Mary C. Looney, George R. Feehery |
|---|---|
| Rok vydání: | 1989 |
| Předmět: |
Site-Specific DNA-Methyltransferase (Adenine-Specific)
Methyltransferase Molecular Sequence Data Flavobacterium Methylation DNA methyltransferase Substrate Specificity chemistry.chemical_compound Recognition sequence Genetics Amino Acid Sequence chemistry.chemical_classification biology Adenine DNA General Medicine Molecular biology FokI In vitro Enzyme Oligodeoxyribonucleotides Biochemistry chemistry biology.protein Chromatography Thin Layer |
| Zdroj: | Gene. 77:1-10 |
| ISSN: | 0378-1119 |
| DOI: | 10.1016/0378-1119(89)90353-3 |
| Popis: | M · Fok I, 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 Fok I recognition sequence: M · Fok I does not methylate single-stranded DNA, nor does it methylate double-stranded DNA at sequences other than Fok I sites. |
| Databáze: | OpenAIRE |
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