Interaction of AluI, Cfr6I and PvuII restriction-modification enzymes with substrates containing either N4-methylcytosine or 5-methylcytosine.

Biochimica et biophysica acta ·Vol. 909 ·No. 3 ·1987-08-25 ·Pages 201-7

Butkus V, Klimasauskas S, Petrauskiene L, Maneliene Z, Lebionka A, Janulaitis A

Abstract

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.

MeSH Terms

5-Methylcytosine Base Sequence Cytosine/analogs & derivatives,metabolism DNA Restriction Enzymes/metabolism DNA, Bacterial/metabolism Deoxyribonucleases, Type II Site-Specific Methylation Substrate Specificity

Chemicals

DNA, Bacterial N(4)-methylcytosine 5-Methylcytosine Cytosine DNA Restriction Enzymes endodeoxyribonuclease AluI CAGCTG-specific type II deoxyribonucleases Deoxyribonucleases, Type II Site-Specific

Authors & Affiliations

6 authors, click to expand affiliations / ORCID

Butkus V

Klimasauskas S

Petrauskiene L

Maneliene Z

Lebionka A

Janulaitis A

Article Info

Journal

Biochimica et biophysica acta

Abbr.

Biochim Biophys Acta

ISSN

0006-3002

DOI

10.1016/0167-4781(87)90078-9

Published

1987-08-25

Pages

201-7

Language

English

Region

Netherlands

NLM ID

0217513

Subset

External Links

PubMed source DOI: 10.1016/0167-4781(87)90078-9

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Interaction of AluI, Cfr6I and PvuII restriction-modification enzymes with substrates containing either N4-methylcytosine or 5-methylcytosine.

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