Autor: |
S. Kh. Degtyarev, D. A. Gonchar, L. N. Golikova, N. A. Netesova, Abdurashitov Ma, Yu. G. Kashirina, Valery A Chernukhin |
Rok vydání: |
2003 |
Předmět: |
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Zdroj: |
Biochemistry (Moscow). 68:967-975 |
ISSN: |
0006-2979 |
Popis: |
The BstF5I restriction–modification system from Bacillus stearothermophilus F5 includes four site-specific DNA methyltransferases, thus differing from all known restriction–modification systems. Here we demonstrated for the first time that one bacterial cell can possess two pairs of methylases with identical substrate specificities (methylases BstF5I-1 and BstF5I-3 recognize GGATG, whereas methylases BstF5I-2 and BstF5I-4 recognize CATCC) that modify adenine residues on both DNA strands. Different chromatographic methods provide homogenous preparations of methylases BstF5I-2 and BstF5I-4. We estimated the principal kinetic parameters of the reaction of transfer of methyl group from the donor S-adenosyl-L-methionine to the recognition site 5"-CATCC-3" catalyzed by BstF5I-2 and BstF5I-4 DNA [N6-adenine]-methyl-transferases from the BstF5I restriction–modification system. |
Databáze: |
OpenAIRE |
Externí odkaz: |
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