Primary structures of mutationally altered ribosomal protein L7/L12 and their effects on cellular growth and translational accuracy.
The amino acid sequences of mutationally altered ribosomal protein L7/L12 from four different rplL mutants of Escherichia coli were determined and correlated with some features of the mutant ribosomes. Two of the rplL mutations are deletions around position 40, which give rise to a shortened hinge region between the two domains of L7/L12. The other two mutants harbor point mutations at position 74 (Gly----Asp) or at position 82 (Glu----Lys), which are in or close to an evolutionarily conserved sequence in the C-terminal domain. The two latter mutations are associated with decreased rates of growth and translational elongation. All four mutants show increased nonsense codon read-through in vivo. Ribosomes from one of the deletion mutants show clearly increased missense error rates in vitro.
D000596:Amino Acids / Q000032:analysis; D001426:Bacterial Proteins / Q000096:biosynthesis / Q000235:genetics; D002851:Chromatography, High Pressure Liquid; D003062:Codon / Q000032:analysis; D003488:Cyanogen Bromide; D004926:Escherichia coli / Q000235:genetics / Q000254:growth & development; D008958:Models, Molecular; D009154:Mutation; D010441:Peptide Chain Elongation, Translational; D010446:Peptide Fragments; D014176:Protein Biosynthesis; D012269:Ribosomal Proteins / Q000235:genetics* / Q000502:physiology; D014357:Trypsin
D000596:Amino Acids; D001426:Bacterial Proteins; D003062:Codon; D010446:Peptide Fragments; D012269:Ribosomal Proteins; C016700:ribosomal protein L7-L12; D014357:Trypsin; D003488:Cyanogen Bromide