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DNA-dependent RNA polymerase II from nuclei of suspension-cultured tobacco cells

✍ Scribed by Jan Szopa; Karl G. Wagner

Publisher
Springer-Verlag
Year
1984
Tongue
English
Weight
1019 KB
Volume
162
Category
Article
ISSN
0032-0935

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✦ Synopsis

From isolated nuclei of suspension cultured cells of Nicotiana tabacum. DNA-dependent RNA polymerase II (E.C. 2.7.76) has been purified to homogeneity as evidenced by polyacrylamidegel electrophoresis under non-denaturing conditions. The purified enzyme had a specific activity of more than 15 nmol min-1.mg-1 with denatured calf thymus DNA as template. Sodium-dodecyl-sulfate gel electrophoresis and protein highperformance liquid chromatography revealed a subunit composition of four proteins with molecular weights of 165000, 135000, 35000 and 25000 and with a stoichiometry of 1:1:2:2. The RNA polymerase did not exhibit any detectable proteinkinase activity. The 25000 subunit binds ADP in a molar ratio of I : 1 ; it could not be decided whether this subunit has an ATPase activity or is merely an acceptor of ADP.

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