Analysis of the stimulatory factor of RNA polymerase II in the initiation and elongation complex.
The interaction between RNA polymerase II and its specific stimulatory factor S-II was studied using each component purified to near homogeneity. It was found that RNA polymerase II and S-II form a complex in the absence of DNA and nucleoside triphosphates, although their interaction was weak. This interaction became stable in the presence of a template and substrates, and a stoichiometric amount of S-II was found to remain in the transcription machinery during RNA chain elongation.
D000818:Animals; D002286:Carcinoma, Ehrlich Tumor / Q000201:enzymology; D004247:DNA / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D006493:Heparin / Q000494:pharmacology; D051379:Mice; D009363:Neoplasm Proteins / Q000378:metabolism*; D012313:RNA / Q000096:biosynthesis; D012319:RNA Polymerase II / Q000378:metabolism*; D013698:Templates, Genetic; D035165:Transcription Factors, General; D014158:Transcription, Genetic; D035602:Transcriptional Elongation Factors
D009363:Neoplasm Proteins; D035165:Transcription Factors, General; D035602:Transcriptional Elongation Factors; C018648:transcription factor S-II; D012313:RNA; D006493:Heparin; D004247:DNA; D012319:RNA Polymerase II