Abortive and productive elongation catalysed by purified spinach chloroplast RNA polymerase.
Experimental conditions are reported under which purified spinach chloroplast RNA polymerase catalyses the abortive elongation reaction on a synthetic poly[d(A-T)] template. The reaction only occurs under very stringent conditions and absolutely requires Mn2+ as the metal activator. No reaction can be detected in the presence of Mg2+. Furthermore, the rate of abortive elongation with the chloroplast enzyme is extremely sensitive to the presence of added salts, such as KCl or (NH4)2SO4, in the reaction assays. In the combined presence of Mn2+ and Mg2+, a marked inhibition of abortive elongation is associated with an activation of productive elongation and an increased length of RNA chains. Thus, whereas Mn2+ is more active than Mg2+ for phosphodiester bond formation, it appears that Mg2+ favors the stabilization of the ternary transcription complexes. These results are compared with those obtained under similar conditions for wheat germ RNA polymerase II and Escherichia coli RNA polymerase.
Job
C
C
Briat
J F
JF
Lescure
A M
AM
Job
D
D
D002384:Catalysis; D002736:Chloroplasts / Q000201:enzymology*; D012321:DNA-Directed RNA Polymerases / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology; D008345:Manganese / Q000494:pharmacology; D009843:Oligoribonucleotides / Q000096:biosynthesis*; D010944:Plants / Q000201:enzymology; D012492:Salts / Q000494:pharmacology; D014908:Triticum / Q000201:enzymology
D009843:Oligoribonucleotides; D012492:Salts; D008345:Manganese; C053104:uridylyl-(3'-5')-adenylyl-(3'-5')uridine; D012321:DNA-Directed RNA Polymerases; D008274:Magnesium