Ribosome Biogenesis: Nonrandom Addition of Structural Proteins to 50 S Subunits
B.H. Sells, Francis C. Davis
Abstract
B.H. Sells, Francis C. Davis
Abstract
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.
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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.
Key concepts: Chloramphenicol, 50S, Ribosome, Ribosomal protein, Leucine, Ribosomal RNA, Escherichia coli, Protein subunit