Purification and properties of the RNA polymerase of an extremely thermophilic bacterium: Thermus aquaticus T2.
The RNA polymerase of the extremely thermophilic bacterium Thermus aquaticus T 2 has been purified to homogeneity. The apparent molecular weights of the subunits of the enzyme are : 165 000, 130000, 92 000 and 44 000. The in vitro temperature optimum of enzyme activity is around 65 degrees C. The enzyme has a preference towards the homologous template and is strongly inhibited by KCI. Rifampicin inhibits the enzyme only to 50% even at very high concentrations. Heparin inhibits it completely, but only at higher molar excess than in the case of the Escherichia coli enzyme. The enzyme can form heparin-resistant complexes at elevated temperatures on the homologous template, but not on E. coli DNA.
D012321:DNA-Directed RNA Polymerases / Q000302:isolation & purification / Q000378:metabolism*; D006088:Gram-Negative Aerobic Bacteria / Q000201:enzymology*; D006493:Heparin / Q000494:pharmacology; D006358:Hot Temperature; D007700:Kinetics; D011189:Potassium Chloride / Q000494:pharmacology; D012293:Rifampin / Q000494:pharmacology
D011189:Potassium Chloride; D006493:Heparin; D012321:DNA-Directed RNA Polymerases; D012293:Rifampin