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. 1993 Feb 25;21(4):987–991. doi: 10.1093/nar/21.4.987

A unique restriction endonuclease, BcgI, from Bacillus coagulans.

H Kong 1, R D Morgan 1, R E Maunus 1, I Schildkraut 1
PMCID: PMC309233  PMID: 8451198

Abstract

We have purified and characterized a new restriction endonuclease, BcgI, which has properties unlike those of the three recognized classes of restriction enzymes. BcgI was isolated from Bacillus coagulans, and it recognizes the sequence CGAN6TGC. BcgI 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 (Kappd) for AdoMet is about 100 nM, while the KappD for sinefungin is about 500 nM.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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