[A new type of cleavage of the recognition site by the site-specific endonuclease Bst 4.4I from Bacillus stearothermophilus 4.4].
A site-specific endonuclease Bst 4.4I was isolated from the cell extract of Bacillus stearothermophilus 4.4 and partially purified by chromatography on Ultragel AcA-44 and heparin-Sepharose. It was shown that the endonuclease cleaves lambda and M13 DNA yielding distinct fragments just as endonucleases of II and III types but, in contrast to them can produce two two-strand cuts separated with 30 to 32 nucleotides in the region of the recognition site.
Kramarov
V M
VM
Fomenkov
A I
AI
Matvienko
N I
NI
D001483:Base Sequence; D002850:Chromatography, Gel; D003090:Coliphages / Q000235:genetics; D004262:DNA Restriction Enzymes / Q000235:genetics / Q000302:isolation & purification*; D004279:DNA, Viral / Q000378:metabolism; D001411:Geobacillus stearothermophilus / Q000201:enzymology*; D006868:Hydrolysis; D008969:Molecular Sequence Data; D010957:Plasmids; D015183:Restriction Mapping
D004279:DNA, Viral; D004262:DNA Restriction Enzymes; C057672:endodeoxyribonuclease Bst4.4I
Novyĭ tip rasshchepleniia uznavaemoĭ posledovatel'nosti nukleotidov saĭt-spetsificheskoĭ éndonukleazoĭ Bst 4.4I iz Bacillus stearothermophilus 4.4.