Skip to main content

Some NLM-NCBI services and products are experiencing heavy traffic, which may affect performance and availability. We apologize for the inconvenience and appreciate your patience. For assistance, please contact our Help Desk at info@ncbi.nlm.nih.gov.

Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1973 Mar;70(3):944–948. doi: 10.1073/pnas.70.3.944

Functional Correspondence Between 30S Ribosomal Proteins of Escherichia coli and Bacillus stearothermophilus*

K Higo 1,2,3, W Held 1,2,3, L Kahan 1,2,3, M Nomura 1,2,3
PMCID: PMC433394  PMID: 4197630

Abstract

30S ribosomal proteins from Bacillus stearothermophilus (B. proteins) have been fractionated and characterized with respect to their ability to replace various E. coli 30S proteins (E. proteins) in the E. coli 30S ribosome reconstitution system. The functional counterparts of all the E. proteins, except S1, S6, S9, and S13, have been tested. In all cases, B. proteins can substitute for E. proteins. Several purified B. proteins are chemically different from their functionally homologous E. proteins. Five B. proteins are immunochemically related to E. proteins; this set includes two proteins that could not be tested in the reconstitution system (S9 and S13). Thus most, if not all, of the E. proteins have functionally equivalent counterparts among B. proteins, even though properties of the two ribosomes are different in several respects. These results suggest that the fundamental structural organization of ribosomes may be the same throughout prokaryotic organisms.

Keywords: ribosome reconstitution, immunochemical crossreaction, protein purification

Full text

PDF
944

Images in this article

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Ambler R. P., Meadway R. J. Chemical structure of bacterial penicillinases. Nature. 1969 Apr 5;222(5188):24–26. doi: 10.1038/222024a0. [DOI] [PubMed] [Google Scholar]
  2. Ansley S. B., Campbell L. L., Sypherd P. S. Isolation and amino acid composition of ribosomal proteins from Bacillus stearothermophilus. J Bacteriol. 1969 May;98(2):568–572. doi: 10.1128/jb.98.2.568-572.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bickle T. A., Traut R. R. Differences in size and number of 80 S and 70 S ribosomal proteins by dodecyl sulfate gel electrophoresis. J Biol Chem. 1971 Nov 25;246(22):6828–6834. [PubMed] [Google Scholar]
  4. Crawford I. P., Yanofsky C. Pseudomonas putida tryptophan synthetase: partial sequence of the subunit. J Bacteriol. 1971 Oct;108(1):248–253. doi: 10.1128/jb.108.1.248-253.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Friedman S. M. Heat stabilities of ribosomal subunits and reassociated ribosomes from Bacillus stearothermophilus. J Bacteriol. 1971 Oct;108(1):589–591. doi: 10.1128/jb.108.1.589-591.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Kaltschmidt E., Wittmann H. G. Ribosomal proteins. VII. Two-dimensional polyacrylamide gel electrophoresis for fingerprinting of ribosomal proteins. Anal Biochem. 1970 Aug;36(2):401–412. doi: 10.1016/0003-2697(70)90376-3. [DOI] [PubMed] [Google Scholar]
  7. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  8. Li S. L., Yanofsky C. Amino acid sequences of fifty residues from the amino termini of the tryptophan synthetase chains of several enterobacteria. J Biol Chem. 1972 Feb 25;247(4):1031–1037. [PubMed] [Google Scholar]
  9. Lodish H. F. Specificity in bacterial protein synthesis: role of initiation factors and ribosomal subunits. Nature. 1970 May 23;226(5247):705–707. doi: 10.1038/226705a0. [DOI] [PubMed] [Google Scholar]
  10. Loening U. E. Molecular weights of ribosomal RNA in relation to evolution. J Mol Biol. 1968 Dec;38(3):355–365. doi: 10.1016/0022-2836(68)90391-4. [DOI] [PubMed] [Google Scholar]
  11. Mizushima S., Nomura M. Assembly mapping of 30S ribosomal proteins from E. coli. Nature. 1970 Jun 27;226(5252):1214–1214. doi: 10.1038/2261214a0. [DOI] [PubMed] [Google Scholar]
  12. Nomura M., Mizushima S., Ozaki M., Traub P., Lowry C. V. Structure and function of ribosomes and their molecular components. Cold Spring Harb Symp Quant Biol. 1969;34:49–61. doi: 10.1101/sqb.1969.034.01.009. [DOI] [PubMed] [Google Scholar]
  13. Nomura M., Traub P., Bechmann H. Hybrid 30S ribosomal particles reconstituted from components of different bacterial origins. Nature. 1968 Aug 24;219(5156):793–799. doi: 10.1038/219793b0. [DOI] [PubMed] [Google Scholar]
  14. Ozaki M., Mizushima S., Nomura M. Identification and functional characterization of the protein controlled by the streptomycin-resistant locus in E. coli. Nature. 1969 Apr 26;222(5191):333–339. doi: 10.1038/222333a0. [DOI] [PubMed] [Google Scholar]
  15. Prager E. M., Wilson A. C. The dependence of immunological cross-reactivity upon sequence resemblance among lysozymes. II. Comparison of precipitin and micro-complement fixation results. J Biol Chem. 1971 Nov 25;246(22):7010–7017. [PubMed] [Google Scholar]
  16. Sherton C. C., Wool I. G. Determination of the number of proteins in liver ribosomes and ribosomal subunits by two-dimensional polyacrylamide gel electrophoresis. J Biol Chem. 1972 Jul 25;247(14):4460–4467. [PubMed] [Google Scholar]
  17. Sun T. T., Bickle T. A., Traut R. R. Similarity in the size and number of ribosomal proteins from different prokaryotes. J Bacteriol. 1972 Aug;111(2):474–480. doi: 10.1128/jb.111.2.474-480.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Taylor M. M., Glasgow J. E., Storck R. Sedimentation coefficients of RNA from 70S and 80S ribosomes. Proc Natl Acad Sci U S A. 1967 Jan;57(1):164–169. doi: 10.1073/pnas.57.1.164. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Wittmann H. G., Stöfflet G., Hindennach I., Kurland C. G., Birge E. A., Randall-Hazelbauer L., Nomura M., Kaltschmidt E., Mizushima S., Traut R. R. Correlation of 30S ribosomal proteins of Escherichia coli isolated in different laboratories. Mol Gen Genet. 1971;111(4):327–333. doi: 10.1007/BF00569784. [DOI] [PubMed] [Google Scholar]
  20. Yoch D. C., Valentine R. C. Ferredoxins and flavodoxins of bacteria. Annu Rev Microbiol. 1972;26:139–162. doi: 10.1146/annurev.mi.26.100172.001035. [DOI] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES