Effects of partial deproteinization on the functional properties of 50S ribosomal subunits of E. coli.
Sedimentation of E. coli 50S ribosomal subunits through sucrose gradients containing 10 mM Mg2+ and high concentrations of NaCl (0.1-1.0 M) leads to removal of proteins L16 and L25. Analyses of the structural and functional properties of the protein depleted particles shows that removal of L16 and L25 from the 50S subunit causes loss of its ability to bind tRNA, to associate with the 30S subunit and to catalyze peptide bond formation. Reassociation of both L16 and L25 with core particles lacking these proteins is necessary for recovery of peptidyl transferase activity.
D002499:Centrifugation, Density Gradient; D004926:Escherichia coli / Q000032:analysis; D010458:Peptidyl Transferases / Q000502:physiology; D012335:RNA, Ribosomal / Q000502:physiology; D012343:RNA, Transfer / Q000502:physiology; D012269:Ribosomal Proteins / Q000502:physiology*; D012270:Ribosomes / Q000502:physiology*; D012965:Sodium Chloride
D012335:RNA, Ribosomal; D012269:Ribosomal Proteins; D012965:Sodium Chloride; D012343:RNA, Transfer; D010458:Peptidyl Transferases