Partial purification of a stimulatory factor of RNA polymerase B in nonhistone proteins; correlation with nuclear protein kinase.
A stimulatory factor of DNA-dependent RNA polymerase B (nucleosidetriphosphate: RNA nucleotidyltransferase, EC 2.7.7.6) in nonhistone proteins was partially purified from rat liver nuclei on a column of daunomycin-CH Sepharose 4B and of phosphocellulose. In the process of purification, the stimulatory factor was separated from the main fraction of nuclear protein kinase (ATP: protein phosphotransferase, EC 2.7.1.37). This factor enhanced specifically the activity of RNA polymerase B on rat liver DNA as template and did not affect RNA polymerase A and Escherichia coli RNA polymerase at all. The polynucleotide elongation rate was increased by the addition of this factor.
D000818:Animals; D002467:Cell Nucleus / Q000201:enzymology*; D002868:Chromosomal Proteins, Non-Histone / Q000032:analysis*; D009363:Neoplasm Proteins / Q000302:isolation & purification*; D011494:Protein Kinases / Q000302:isolation & purification*; D012313:RNA / Q000096:biosynthesis; D051381:Rats; D014157:Transcription Factors / Q000302:isolation & purification*; D035165:Transcription Factors, General; D035602:Transcriptional Elongation Factors
D002868:Chromosomal Proteins, Non-Histone; D009363:Neoplasm Proteins; D014157:Transcription Factors; D035165:Transcription Factors, General; D035602:Transcriptional Elongation Factors; C018648:transcription factor S-II; D012313:RNA; D011494:Protein Kinases