This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Higo, K.-I. Articles by Loertscher, K. Search for Related Content PubMed PubMed Citation Articles by Higo, K.-I. Articles by Loertscher, K.

Amino-Terminal Sequences of Some Escherichia coli 30S Ribosomal Proteins and Functionally Corresponding Bacillus stearothermophilus Ribosomal Proteins¹

^a Institute for Enzyme Research and Department of Genetics, University of Wisconsin, Madison, Wisconsin 53706

ABSTRACT

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.

¹ Paper no. 1707 of the Laboratory of Genetics, University of Wisconsin, Madison, Wis. 53706.