Characterization of BcgI, a new kind of restriction-modification system
The BcgI restriction enzyme from Bacillus coagulans is unusual in that it cleaves on both sides of its recognition site, CGAN6TGC, releasing a fragment that includes the site and several bases on each side. We report the organization and nucleotide sequences of the genes for the BcgI restriction-mod...
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Published in: | The Journal of biological chemistry Vol. 269; no. 1; pp. 683 - 690 |
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Main Authors: | , , , , , |
Format: | Journal Article |
Language: | English |
Published: |
Bethesda, MD
American Society for Biochemistry and Molecular Biology
07-01-1994
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Subjects: | |
Online Access: | Get full text |
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Summary: | The BcgI restriction enzyme from Bacillus coagulans is unusual in that it cleaves on both sides of its recognition site, CGAN6TGC,
releasing a fragment that includes the site and several bases on each side. We report the organization and nucleotide sequences
of the genes for the BcgI restriction-modification system and the properties of the proteins that they encode. The system
comprises two adjacent, similarly oriented genes. The proximal gene, bcgIA, codes for a 637-amino acid protein (molecular
mass = 71.6 kDa) that resembles certain m6A-specific DNA-methyltransferases, particularly those that constitute the modification
subunits of type I restriction-modification systems. The distal gene, bcgIB, codes for a 341-amino acid protein (molecular
mass = 39.2 kDa) that resembles none of the sequences in the sequence data bases. The two genes overlap by several nucleotides.
Alone, neither protein restricts or modifies DNA, but, together, they form a complex in the proportion A2B that does both.
DNA binding assays showed that the DNA-protein complex can be formed only in the presence of both subunits, suggesting that
the association of inactive subunits generates the active BcgI enzyme that can bind DNA and then either cleaves or methylates
at target site. |
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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 |
ISSN: | 0021-9258 1083-351X |
DOI: | 10.1016/S0021-9258(17)42403-3 |