BCOAI, A NEW SITE-SPECIFIC ENDONUCLEASE FROM BACILLUS-COAGULANS

被引：0
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作者：
SOKOLOV, NN [1 ]
ELDAROV, MA [1 ]
ANIKEITCHEVA, NV [1 ]
KARPYCHEV, IV [1 ]
SAMKO, OT [1 ]
FITZNER, AB [1 ]
KALUGIN, AA [1 ]
CHOROSHOUTINA, EB [1 ]
SKRYABIN, KG [1 ]
机构：
[1] VA ENGELHARDT MOLEC BIOL INST,CTR BIOENGN,MOSCOW,USSR
来源：
BIOORGANICHESKAYA KHIMIYA | 1991年 / 17卷 / 09期
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摘要：
A new site-specific endonuclease was detected in toluene lysates of Bacillus coagulans AUCM B-732 and designated as BcoAI. The enzyme was purified by fractionation of the cell-free extract in the two-phase PEG/dextran system followed by chromatography on DEAE-sepharose and phosphocellulose and shown to be free of nonspecific nucleases and phosphatases. BcoAI has three cleavage sites on lambda-DNA, but does not cleave SV40, pBR322 and pUC19 DNA. BcoAI recognizes the sequence 5' CAC down GTG 3' on double-stranded DNA and cleaves it as indicated by the arrow to yield blunt-ended DNA fragments. Thus, BcoAI is a true isoschizomer of PmaCI from Pseudomonas maltophila C.
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页码：1188 / 1192
页数：5
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