Skip to main content
NCBI home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1973 Nov;116(2):757–763. doi: 10.1128/jb.116.2.757-763.1973

Comparison of the Activities of Extracts of Escherichia coli and Salmonella typhimurium in Amino Acid Incorporation

B A Bassel 1, M E Curry 1
PMCID: PMC285442  PMID: 4583250

Abstract

We have compared the amino acid incorporating activities of extracts of Escherichia coli and Salmonella typhimurium in in vitro protein-synthesizing systems directed by bacterial messenger ribonucleic acid (mRNA) of both species and by the genomes of coliphages Qβ and f2. E. coli and S. typhimurium extracts translate both homologous and heterologous bacterial mRNAs at comparable rates. S. typhimurium extracts translate phage RNAs only 10 to 15% as fast as E. coli extracts do. The presence of glucose in the growth medium increases the activity of S. typhimurium extracts three- to fourfold in the phage RNA-directed systems. Glucose has a much more limited effect on the activities of E. coli extracts. We show that similar amounts of phage RNA-ribosome complexes are formed in both the E. coli and the S. typhimurium systems, indicating that the different activities observed may be attributed to different rates of peptide elongation or to the formation of complexes at different sites on the RNA strand.

Full text

PDF
757

Selected References

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

  1. Bassel B. A., Jr Cell-free protein synthesis directed by Q beta-RNA and by two specific fragments. Proc Natl Acad Sci U S A. 1968 May;60(1):321–328. doi: 10.1073/pnas.60.1.321. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. GIERER A., SCHRAMM G. Infectivity of ribonucleic acid from tobacco mosaic virus. Nature. 1956 Apr 14;177(4511):702–703. doi: 10.1038/177702a0. [DOI] [PubMed] [Google Scholar]
  3. Gesteland R. F. Isolation and characterization of ribonuclease I mutants of Escherichia coli. J Mol Biol. 1966 Mar;16(1):67–84. doi: 10.1016/s0022-2836(66)80263-2. [DOI] [PubMed] [Google Scholar]
  4. Himes R. H., Stallcup M. R., Rabinowitz J. C. Translation of synthetic and endogenous messenger ribonucleic acid in vitro by ribosomes and polyribosomes from Clostridium pasteurianum. J Bacteriol. 1972 Dec;112(3):1057–1069. doi: 10.1128/jb.112.3.1057-1069.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Howk R., Sarimo S. S., Pine M. J. Translation of RNA coliphages by amino acid-incorporation systems of the Enterobacteriaceae. J Gen Microbiol. 1973 Jan;74(1):93–96. doi: 10.1099/00221287-74-1-93. [DOI] [PubMed] [Google Scholar]
  6. Konigsberg W., Maita T., Katze J., Weber K. Amino-acid sequence of the "Qbeta" coat protein. Nature. 1970 Jul 18;227(5255):271–273. doi: 10.1038/227271a0. [DOI] [PubMed] [Google Scholar]
  7. LOEB T., ZINDER N. D. A bacteriophage containing RNA. Proc Natl Acad Sci U S A. 1961 Mar 15;47:282–289. doi: 10.1073/pnas.47.3.282. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Lodish H. F., Robertson H. D. Regulation of in vitro translation of bacteriophage f2 RNA. Cold Spring Harb Symp Quant Biol. 1969;34:655–673. doi: 10.1101/sqb.1969.034.01.076. [DOI] [PubMed] [Google Scholar]
  9. Lodish H. F. Species specificity of polypeptide chain initiation. Nature. 1969 Nov 29;224(5222):867–870. doi: 10.1038/224867a0. [DOI] [PubMed] [Google Scholar]
  10. 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]
  11. Min Jou W., Haegeman G., Ysebaert M., Fiers W. Nucleotide sequence of the gene coding for the bacteriophage MS2 coat protein. Nature. 1972 May 12;237(5350):82–88. doi: 10.1038/237082a0. [DOI] [PubMed] [Google Scholar]
  12. NIRENBERG M. W., MATTHAEI J. H. The dependence of cell-free protein synthesis in E. coli upon naturally occurring or synthetic polyribonucleotides. Proc Natl Acad Sci U S A. 1961 Oct 15;47:1588–1602. doi: 10.1073/pnas.47.10.1588. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Noll H. Characterization of macromolecules by constant velocity sedimentation. Nature. 1967 Jul 22;215(5099):360–363. doi: 10.1038/215360a0. [DOI] [PubMed] [Google Scholar]
  14. OHTAKA Y., SPIEGELMAN S. TRANSLATIONAL CONTROL OF PROTEIN SYNTHESIS IN A CELL-FREE SYSTEM DIRECTED BY A POLYCISTRONIC VIRAL RNA. Science. 1963 Oct 25;142(3591):493–497. doi: 10.1126/science.142.3591.493. [DOI] [PubMed] [Google Scholar]
  15. Stallcup M. R., Rabinowitz J. C. Initiation of protein synthesis in vitro by a clostridial system. I. Specificity in the translation of natural messenger ribonucleic acids. J Biol Chem. 1973 May 10;248(9):3209–3215. [PubMed] [Google Scholar]
  16. Stallcup M. R., Rabinowitz J. C. Initiation of protein synthesis in vitro by a clostridial system. II. The roles of initiation factors and salt-washed ribosomes in determining specificity in the translation of natural messenger ribonucleic acids. J Biol Chem. 1973 May 10;248(9):3216–3219. [PubMed] [Google Scholar]
  17. Sugiyama T., Hebert R. R., Hartman K. A. Ribonucleoprotein complexes formed between bacteriophage MS2 RNA and MS2 protein in vitro. J Mol Biol. 1967 May 14;25(3):455–463. doi: 10.1016/0022-2836(67)90198-2. [DOI] [PubMed] [Google Scholar]
  18. Szer W., Brenowitz J. Translation of MS2 RNA by ribosomes from different bacterial species. Biochem Biophys Res Commun. 1970 Mar 27;38(6):1154–1160. doi: 10.1016/0006-291x(70)90360-8. [DOI] [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES