| Autor: |
Chernukhin VA; Institute of Molecular Biology and Biophysics, Siberian Division, Russian Academy of Medical Sciences, Novosibirsk 630117, Russia., Golikova LN, Gonchar DA, Abdurashitov MA, Kashirina YG, Netesova NA, Degtyarev SKh |
| Jazyk: |
angličtina |
| Zdroj: |
Biochemistry. Biokhimiia [Biochemistry (Mosc)] 2003 Sep; Vol. 68 (9), pp. 967-75. |
| DOI: |
10.1023/a:1026004427401 |
| Abstrakt: |
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]-methyltransferases from the BstF5I restriction-modification system. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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