In vitro synthesis of the delta-lysin of Staphylococcus aureus.
The stability of mRNA for the delta-lysin of Staphylococcus aureus was determined by measuring the residual lysin synthesis after inhibition of DNA-dependent RNA polymerase activity with rifampin. At the late logarithmic-early stationary phase of growth the delta-lysin mRNA was very stable, with a half-life of ca. 20 min. Total cellular RNA was extracted from S. aureus and translated with a modified Escherichia coli S-30 system; delta-lysin was identified amongst the translation products by immunoprecipitation and immunoabsorption. The delta-lysin synthesized in vitro was of a size similar to mature delta-lysin and did not require a signal sequence for secretion from the cell.
D001426:Bacterial Proteins / Q000235:genetics* / Q000302:isolation & purification; D002474:Cell-Free System; D012321:DNA-Directed RNA Polymerases / Q000037:antagonists & inhibitors; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000235:genetics; D006460:Hemolysin Proteins; D007700:Kinetics; D014176:Protein Biosynthesis; D012329:RNA, Bacterial / Q000235:genetics; D012333:RNA, Messenger / Q000235:genetics; D012293:Rifampin / Q000633:toxicity; D013211:Staphylococcus aureus / Q000187:drug effects / Q000378:metabolism*
D001426:Bacterial Proteins; D006460:Hemolysin Proteins; D012329:RNA, Bacterial; D012333:RNA, Messenger; C025994:delta hemolysin protein, Staphylococcus aureus; D012321:DNA-Directed RNA Polymerases; D012293:Rifampin