Heat shock protein stimulates in vitro transcription of nitrogen regulator gene glnL of Escherichia coli.
The in vitro transcription of glnL, initiated at the gene's specific promoter, was stimulated by adding a proteinaceous fraction purified from a culture at 42 degrees C, while the corresponding fraction from a culture at 28 degrees C was not stimulating. The stimulating fraction was not effective on in vitro transcription of some other genes. These stimulating and nonstimulating fractions were further purified and comparatively analyzed in sodium dodecyl sulfate polyacrylamide gel electrophoresis, which revealed that the amounts of 84 kD protein had predominantly increased in the stimulating fraction, but not in the nonstimulating fraction.
D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000235:genetics*; D006360:Heat-Shock Proteins / Q000502:physiology*; D009584:Nitrogen / Q000378:metabolism; D010749:Phosphoprotein Phosphatases / Q000235:genetics*; D011494:Protein Kinases / Q000235:genetics*; D012333:RNA, Messenger / Q000235:genetics; D014158:Transcription, Genetic / Q000502:physiology*