Amino-terminal sequences of some Escherichia coli 30S ribosomal proteins and functionally corresponding Bacillus stearothermophilus ribosomal proteins.
Amino-terminal sequences of five purified Escherichia coli 30S ribosomal proteins (S4, S9, S10, S16, and S20) were compared with those of their functionally corresponding Bacillus stearothermophilus ribosomal proteins identified previously by the reconstitution technique. An automatic Edman degradation method was used for sequence determinations. The sequence of the first 30 residues is presented, except that only the first 25 residues are shown for the S20 pair. Substantial (40 to 70%) sequence homologies have been observed in every case. The results show that the pairs of functionally equivalent proteins, previously identified by the reconstitution technique, are also chemically related. Thus, the present chemical studies give further support for the previous conclusion that two ribosomes with different properties, 30S subunits from E. coli and B. stearothermophilus, have the same fundamental structural organization.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis*; D001407:Bacillus / Q000032:analysis*; D001426:Bacterial Proteins / Q000032:analysis*; D002849:Chromatography, Gas; D002852:Chromatography, Ion Exchange; D002855:Chromatography, Thin Layer; D004926:Escherichia coli / Q000032:analysis*; D012270:Ribosomes / Q000032:analysis*
D000596:Amino Acids; D001426:Bacterial Proteins