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  • Title: [Covalent binding of Cys142 from SsoII methyltransferase with DNA duplexes, containing a phosphoryldisulfide internucleotide group].
    Author: Vorob'eva OV, Romanenkov AS, Metelev VG, Kariagina AS, Lavrova NV, Oretskaia TS, Kubareva EA.
    Journal: Mol Biol (Mosk); 2003; 37(5):906-15. PubMed ID: 14593929.
    Abstract:
    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.
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