[Effect of the structure of oligonucleotide substrates on interaction with methylase Eco dam].
The interaction of Eco dam methylase with various synthetic oligonucleotide substrates was investigated. The "imperfect" duplexes contained a normal GATC recognition sequence in one chain of the enzyme recognition site and had some defects in the complementary chain, i.e., the absence of one or several nucleotide residues or the presence of S-methyl thiophosphate groups at the 3'-termini. The 3'-S-methyl thiophosphate residue has the same effect on the methylation of oligonucleotide complexes as does the absence of internucleotide phosphate in the analogous complexes. The presence of both GA dinucleotides in the recognition site is necessary for a productive enzyme-substrate interaction. The experimental data suggest that Eco dam methylase does form a symmetrical enzyme-substrate complex which is similar to that formed by type II restriction enzymes.
Malygin
E G
EG
Zinov'ev
V V
VV
Gorbunov
Iu A
IuA
Popov
S G
SG
Rechkunova
N I
NI
D001483:Base Sequence; D004591:Electrophoresis, Polyacrylamide Gel; D008745:Methylation; D008780:Methyltransferases / Q000378:metabolism*; D009690:Nucleic Acid Conformation; D009838:Oligodeoxyribonucleotides / Q000138:chemical synthesis / Q000378:metabolism*; D015265:Site-Specific DNA-Methyltransferase (Adenine-Specific); D013379:Substrate Specificity
D009838:Oligodeoxyribonucleotides; D008780:Methyltransferases; C058693:Dam methyltransferase; D015265:Site-Specific DNA-Methyltransferase (Adenine-Specific)
Vliianie struktury oligonukleotidnykh substratov na vzaimodeĭstvie s metilazoĭ Eco dam.