Properties of unprimed poly(A)-poly(U) synthesis by Caulobacter crescentus RNA polymerase.
Some properties of unprimed poly(A)-poly(U) synthesis by DNA-dependent RNA polymerase from Caulobacter crescentus were examined. The reaction required ATP and UTP as substrates and manganese as a divalent cation. Rifampicin completely inhibited the reaction at a concentration of 1 micron/ml, and the enzyme catalyzed the polymer synthesis well regardless of the presence of GTP, CTP or both. The chain length of the poly(A)-poly(U) synthesized was about one hundred base pairs, as estimated from a sedimentation velocity and the molar ratio of [3H]AMP to [gamma-32P]ATP incorporated into the poly(A)-poly(U). The reaction was dependent on the square of the enzyme concentration and the enzyme dimers formed complexes with poly(A)-poly(U) during the reaction.
D000249:Adenosine Monophosphate / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D003570:Cytidine Triphosphate / Q000378:metabolism; D012321:DNA-Directed RNA Polymerases / Q000378:metabolism*; D006088:Gram-Negative Aerobic Bacteria / Q000201:enzymology*; D006160:Guanosine Triphosphate / Q000378:metabolism; D007700:Kinetics; D008345:Manganese / Q000378:metabolism; D008970:Molecular Weight; D011063:Poly A-U / Q000096:biosynthesis*; D012293:Rifampin / Q000494:pharmacology; D014544:Uridine Triphosphate / Q000378:metabolism
D011063:Poly A-U; D000249:Adenosine Monophosphate; D008345:Manganese; D003570:Cytidine Triphosphate; D006160:Guanosine Triphosphate; D000255:Adenosine Triphosphate; D012321:DNA-Directed RNA Polymerases; D014544:Uridine Triphosphate; D012293:Rifampin