[Covalent binding of Cys142 from SsoII methyltransferase with DNA duplexes, containing a phosphoryldisulfide internucleotide group].
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.
Chemical Department, Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow, 119992 Russia.
O V
OV
Vorob'eva
A S
AS
Romanenkov
V G
VG
Metelev
A S
AS
Kariagina
N V
NV
Lavrova
T S
TS
Oretskaia
E A
EA
Kubareva
D000595:Amino Acid Sequence; D001483:Base Sequence; D003545:Cysteine / Q000378:metabolism*; D004247:DNA / Q000737:chemistry / Q000378:metabolism*; D019175:DNA Methylation; D015257:DNA-Cytosine Methylases / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009943:Organophosphorus Compounds / Q000378:metabolism*; D011485:Protein Binding; D017386:Sequence Homology, Amino Acid
D009943:Organophosphorus Compounds; D004247:DNA; C063974:DNA modification methylase SsoII; D015257:DNA-Cytosine Methylases; D003545:Cysteine