Ribosome biogenesis: nonrandom addition of structural proteins to 50S subunits.
Assemblage of structural proteins into 50S subunits was examined in Escherichia coli recovering fromt chloramphenicol treatment. Cells previously labeled with H3-leucine for three generations were incuibated for 30 minutes with chloramnlphenicol. Proteins synthesized during the initial 5 minuites of recovery from chlorarmphenicol treatmnent were labeled with C(14)-leucine. Marked variation in the ratios of C(14)- to H(3)-leucine in ribosomal protein occurred in cells that had been treated with chloramphenicol; luntreated cells displayed little variation. Thle resuilts sliggest that ribosomal proteins are assenmbled into 50S subunits in a nonrandom manner.
D001426:Bacterial Proteins / Q000096:biosynthesis* / Q000302:isolation & purification; D002247:Carbon Isotopes; D002701:Chloramphenicol / Q000494:pharmacology; D004589:Electrophoresis, Disc; D004926:Escherichia coli / Q000166:cytology / Q000378:metabolism*; D007930:Leucine / Q000378:metabolism; D012270:Ribosomes / Q000187:drug effects / Q000378:metabolism*; D014316:Tritium
D001426:Bacterial Proteins; D002247:Carbon Isotopes; D014316:Tritium; D002701:Chloramphenicol; D007930:Leucine