New site site-specific endonuclease and methylase from Bacillus licheniformis 736

The site-specific endonuclease R Bli736I and methylase M Bli736I have been isolated from the Bacillus licheniformis strain 736 by blue-agarose, hydroxyapatite-Ultragel and heparin-Sepharose chromatography. The enzymes are free from interfering impurities. R Bli736I recognizes the 5'-GGTCTCN-3&#...

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Bibliographic Details
Published inBiokhimiia (Moscow, Russia) Vol. 58; no. 8; p. 1139
Main Authors Matvienko, N N, Kramarov, V M, Zheleznaia, L A, Matvienko, N I
Format Journal Article
LanguageRussian
Published Russia (Federation) 01.08.1993
Subjects
Bacillus - enzymology
Base Sequence
Chromatography, Gel
Deoxyribonucleases, Type II Site-Specific - isolation & purification
Deoxyribonucleases, Type II Site-Specific - metabolism
DNA, Viral - metabolism
DNA-Cytosine Methylases - isolation & purification
DNA-Cytosine Methylases - metabolism
Electrophoresis, Agar Gel
Molecular Sequence Data
Site-Specific DNA-Methyltransferase (Adenine-Specific) - isolation & purification
Site-Specific DNA-Methyltransferase (Adenine-Specific) - metabolism
Substrate Specificity
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Summary:The site-specific endonuclease R Bli736I and methylase M Bli736I have been isolated from the Bacillus licheniformis strain 736 by blue-agarose, hydroxyapatite-Ultragel and heparin-Sepharose chromatography. The enzymes are free from interfering impurities. R Bli736I recognizes the 5'-GGTCTCN-3' decreases and decreases 5'-NNNNNGAGACC-3' sequences on the DNA and cleaves the DNA as indicated by arrows to form single-stranded 4-nucleotide 5'-protruding termini. This enzyme is an isoschizomer of Eco3II isolated from E. coli.
ISSN:0320-9725