[Effect of 5-azacytidine on E. coli cells with different DNA-methylases].
A correlation was found between the bacteriocide effect of 5-aza-C and the amount of cytosine DNA-methylases in E. coli cells. 5-Aza-C-DNA induced partial or complete inhibition of bacterial DNA-methylases with different site specificity; cytosine DNA-methylases were inhibited by the DNA more effectively than adenine DNA-methylase Eco dam. The inhibitory influence of 5-aza-C-DNA on cytosine DNA-methylases was due to the formation of stable inactive complexes between the enzyme and the non-methylating cytosine analog in the recognition sites. Cytosine DNA-methylase Eco RII formed a relatively firm bond with 5-aza-C-DNA, which could be disrupted by 1 M KCl; this disruption restores the DNA-methylase activity and the inhibiting capacity of 5-aza-C-DNA. Thus, the binding of cytosine DNA-methylase to 5-aza-C in DNA is noncovalent; the inhibition of the enzyme by 5-aza-C-DNA is reversible.
M T
MT
Venozhinskis
V F
VF
Nesterenko
S I
SI
Kanopkaĭte
Ia I
IaI
Bur'ianov
D001374:Azacitidine / Q000494:pharmacology*; D004248:DNA (Cytosine-5-)-Methyltransferases / Q000037:antagonists & inhibitors*; D015257:DNA-Cytosine Methylases; D004926:Escherichia coli / Q000187:drug effects / Q000201:enzymology*; D008780:Methyltransferases / Q000037:antagonists & inhibitors*; D015265:Site-Specific DNA-Methyltransferase (Adenine-Specific)
C029528:DNA modification methylase EcoRII; D015257:DNA-Cytosine Methylases; D008780:Methyltransferases; D004248:DNA (Cytosine-5-)-Methyltransferases; D015265:Site-Specific DNA-Methyltransferase (Adenine-Specific); D001374:Azacitidine
Deĭstvie 5-azatsitidina na kletki E. coli s razlichnymi DNK-metilazami.