| Autor: |
Vorob'eva OV; Chemical Department, Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow, 119992 Russia., Romanenkov AS, Metelev VG, Kariagina AS, Lavrova NV, Oretskaia TS, Kubareva EA |
| Jazyk: |
ruština |
| Zdroj: |
Molekuliarnaia biologiia [Mol Biol (Mosk)] 2003 Sep-Oct; Vol. 37 (5), pp. 906-15. |
| Abstrakt: |
DNA duplexes containing a single phosphoryldisulfide link in place of the natural internucleotide phosphodiester bond were employed in affinity modification of Cys142 in cytosine-C5 DNA methyltransferase SsoII (M.SsoII). The possibility of duplex-M.SsoII conjugation as a result of disulfide exchange was demonstrated. The crosslinking efficiency proved to depend on the DNA primary structure, modification position, and the presence of S-adenosyl-L-homocysteine, a nonreactive analog of the methylation cofactor. The SH group of M.SsoII Cys142 was assumed to be close to the DNA sugar-phosphate backbone in the DNA-enzyme complex. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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