Interaction of AluI, Cfr6I and PvuII restriction-modification enzymes with substrates containing either N4-methylcytosine or 5-methylcytosine
| Autor: | Arvydas Janulaitis, Z. Manelien, V. Butkus, L. Petrauskien, Saulius Klimašauskas, A. Lebionka |
|---|---|
| Rok vydání: | 1987 |
| Předmět: |
DNA
Bacterial chemistry.chemical_classification Base Sequence Biophysics DNA Restriction Enzymes Methylation Biology Cleavage (embryo) Biochemistry Molecular biology Substrate Specificity Cytosine 5-Methylcytosine chemistry.chemical_compound Restriction enzyme Enzyme chemistry Structural Biology Isoschizomer Genetics Substrate specificity Deoxyribonucleases Type II Site-Specific |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 909:201-207 |
| ISSN: | 0167-4781 |
| DOI: | 10.1016/0167-4781(87)90078-9 |
| Popis: | The cleavage specificity of R.Cfr6I, an isoschizomer of PvuII restriction endonuclease was determined to be 5'CAG decreases CTG and the methylation specificity of Cfr6I and PvuII methylases, 5'CAG4mCTG. Thus, M.Cfr6I and M.PvuII are new additions to the list of methylases with N4-methylcytosine specificity. Neither of the above RM enzymes acts on the substrates containing either N4-methylcytosine or 5-methylcytosine in a cognate methylation position. |
| Databáze: | OpenAIRE |
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