A UNIQUE RESTRICTION ENDONUCLEASE, BCGI, FROM BACILLUS-COAGULANS

作者：KONG HM; MORGAN RD; MAUNUS RE; SCHILDKRAUT I

来源：Nucleic Acids Research, 1993, 21(4): 987-991.

DOI：10.1093/nar/21.4.987

We have purified and characterized a new restriction endonuclease, Bcgl, which has properties unlike those of the three recognized classes of restriction enzymes. Bcgl was isolated from Bacillus coagulans, and it recognizes the sequence CGAN6TGC. Bcgl cleaves double stranded DNA on both strands upstream and downstream of the recognition sequence, so that the recognition sequence is released as a 34-base pair fragment with 2-base 3'-extensions. Mg++ and S-adenosylmethionine are required for cleavage. Sinefungin, a structural analogue of AdoMet which generally inhibits methylase activity, can replace AdoMet in the cleavage reaction. The apparent binding constant (K(b)app) for AdoMet is about 100 nM, while the K(b)app for sinefungin is about 500 nM.

• 出版日期1993-2-25
• 单位New England Biolabs