Selective inhibition of RNase H by dextran.
Ordinarily, ribonuclease H hydrolyzes poly(rA) . poly(dT) and phiX174DNA-RNA at equal rates. Here we show that in the presence of dextran, the degradation of poly(rA) . poly(dT) is inhibited, while that of phi 174DNA-RNA is not. A similar inhibition by sucrose is found to be due to trace contamination of dextran in the sucrose. Ribose, deoxyribose, and a number of other saccharides fail to inhibit RNase H. In experiments where the two substrates are presented in the presence of the inhibitor, the kinetics indicates that both molecules are recognized by the enzyme, but only the phi X174DNA-RNA is degraded. That is, dextran does not interfere with the recognition site, but rather blocks hydrolysis. It is proposed that the ability of dextran to confer selectivity toward different substrates reveals a potential regulatory mechanism for RNase H activity which may represent a control step in the initiation of DNA synthesis.
D003911:Dextrans / Q000494:pharmacology*; D004720:Endonucleases / Q000037:antagonists & inhibitors*; D004926:Escherichia coli / Q000201:enzymology; D007700:Kinetics; D016914:Ribonuclease H; D012260:Ribonucleases / Q000037:antagonists & inhibitors*; D013329:Structure-Activity Relationship; D013379:Substrate Specificity; D013395:Sucrose / Q000494:pharmacology
D003911:Dextrans; D013395:Sucrose; D004720:Endonucleases; D012260:Ribonucleases; D016914:Ribonuclease H