Covalent binding of Cys142 from SsoII methyltransferase with DNA duplexes, containing a phosphoryldisulfide internucleotide group |
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| Authors: | Vorob'eva O V Romanenkov A S Metelev V G Kariagina A S Lavrova N V Oretskaia T S Kubareva E A |
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| Institution: | Chemical Department, Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow, 119992 Russia. |
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| 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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