Functional hybrid enzymes reconstituted from Escherichia coli and Serratia marcescens RNA polymerase subunits.
RNA polymerase was isolated from Escherichia coli and Serratia marcescens. The subunits of both enzymes were separated by electrophoresis on cellulose acetate sheets in the presence of urea. Under conditions favouring reconstitution of the RNA polymerases, stoichiometric amounts of the subunits were allowed to interact. Active hybrid enzymes were formed if corresponding subunits of both enzymes were mutually exchanged. The analysis of the RNA products synthesized showed that the reconstituted enzymes are able to recognize the promoters for transcription and the termination signals on the DNA template. The transcription products can serve as messengers for cell-free protein synthesis.
D001665:Binding Sites; D003090:Coliphages / Q000378:metabolism; D012321:DNA-Directed RNA Polymerases / Q000302:isolation & purification / Q000378:metabolism*; D004926:Escherichia coli / Q000187:drug effects / Q000201:enzymology*; D005696:Galactosidases / Q000096:biosynthesis; D046911:Macromolecular Substances; D011485:Protein Binding; D014176:Protein Biosynthesis; D012293:Rifampin / Q000494:pharmacology; D012706:Serratia marcescens / Q000187:drug effects / Q000201:enzymology*; D014158:Transcription, Genetic; D014508:Urea
D046911:Macromolecular Substances; D014508:Urea; D012321:DNA-Directed RNA Polymerases; D005696:Galactosidases; D012293:Rifampin