Skip to main content
PMC home page
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
. 1975 Aug;72(8):2940–2944. doi: 10.1073/pnas.72.8.2940

Binding of ribosomal protein S1 of Escherichia coli to the 3' end of 16S rRNA.

A E Dahlberg, J E Dahlberg
PMCID: PMC432894  PMID: 1103129

Abstract

Ribosomal protein S1 reversibly binds the 49-nucleotide fragment that is cleaved from the 3' end of 16S rRNA in ribosomes by colicin E3. The fragment has secondary structure in the form of a hairpin loop. At the base of the stem is a sequence (A-C-C-U-C-C) thought to be involved in the base pairing with complementary sequences in mRNA during the initiation of protein synthesis. The role of S1 may be to stabilize this region of the fragment in an open conformation to allow for base pairing to mRNA. This model is supported by the observation that S1 binds specifically to this region of the fragment. In addition, aurin tricarboxylic acid, an inhibitor of protein synthesis, reverses this effect by disrupting the S1-RNA complex. These results can explain why S1 is an essential component of the ribosome for translation of natural mRNA and why aurin tricarboxylic acid blocks initiation.

Full text

PDF
2942

Images in this article

2941Image
on p.2941
2942Image
on p.2942
2942Image
on p.2942
2942Image
on p.2942

Selected References

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

  1. Bowman C. M., Dahlberg J. E., Ikemura T., Konisky J., Nomura M. Specific inactivation of 16S ribosomal RNA induced by colicin E3 in vivo. Proc Natl Acad Sci U S A. 1971 May;68(5):964–968. doi: 10.1073/pnas.68.5.964. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Dahlberg A. E. Two forms of the 30 S ribosomal subunit of Escherichia coli. J Biol Chem. 1974 Dec 10;249(23):7673–7678. [PubMed] [Google Scholar]
  3. Dahlberg J. E. Terminal sequences of bacteriophage RNAs. Nature. 1968 Nov 9;220(5167):548–552. doi: 10.1038/220548a0. [DOI] [PubMed] [Google Scholar]
  4. Ehresmann C., Stiegler P., Mackie G. A., Zimmermann R. A., Ebel J. P., Fellner P. Primary sequence of the 16S ribosomal RNA of Escherichia coli. Nucleic Acids Res. 1975 Feb;2(2):265–278. doi: 10.1093/nar/2.2.265. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Feldman M. Y. Reactions of nucleic acids and nucleoproteins with formaldehyde. Prog Nucleic Acid Res Mol Biol. 1973;13:1–49. doi: 10.1016/s0079-6603(08)60099-9. [DOI] [PubMed] [Google Scholar]
  6. Fiser I., Scheit K. H., Stöffler G., Kuechler E. Identification of protein S 1 at the messenger RNA binding site of the Escherichia coli ribosome. Biochem Biophys Res Commun. 1974 Oct 8;60(3):1112–1118. doi: 10.1016/0006-291x(74)90427-6. [DOI] [PubMed] [Google Scholar]
  7. Goldberg M. L., Steitz J. A. Cistron specificity of 30S ribosomes heterologously reconstituted with components from Escherichia coli and Bacillus stearothermophilus. Biochemistry. 1974 May 7;13(10):2123–2129. doi: 10.1021/bi00707a020. [DOI] [PubMed] [Google Scholar]
  8. Held W. A., Gette W. R., Nomura M. Role of 16S ribosomal ribonucleic acid and the 30S ribosomal protein S12 in the initiation of natural messenger ribonucleic acid translation. Biochemistry. 1974 May 7;13(10):2115–2122. doi: 10.1021/bi00707a019. [DOI] [PubMed] [Google Scholar]
  9. Kenner R. A. A protein-nucleic acid crosslink in 30S ribosomes. Biochem Biophys Res Commun. 1973 Apr 16;51(4):932–938. doi: 10.1016/0006-291x(73)90016-8. [DOI] [PubMed] [Google Scholar]
  10. Landy A., Abelson J., Goodman H. M., Smith J. D. Specific hybridization of tyrosine transfer ribonucleic acids with DNA from a transducing bacteriophage phi-80 carrying the amber suppressor gene su 3. J Mol Biol. 1967 Nov 14;29(3):457–471. doi: 10.1016/0022-2836(67)90112-x. [DOI] [PubMed] [Google Scholar]
  11. Lindahl L., Forchhammer J. Evidence for reduced breakdown of messenger RNA during blocked transcription or translation in Escherichia coli. J Mol Biol. 1969 Aug 14;43(3):593–606. doi: 10.1016/0022-2836(69)90361-1. [DOI] [PubMed] [Google Scholar]
  12. Lodish H. F. Thermal melting of bacteriophage f2 RNA and initiation of synthesis of the maturation protein. J Mol Biol. 1971 Mar 28;56(3):627–632. doi: 10.1016/0022-2836(71)90406-2. [DOI] [PubMed] [Google Scholar]
  13. Miller M. J., Wahba A. J. Inhibition of synthetic and natural messenger translation. II. Specificity and mechanism of action of a protein isolated from Escherichia coli MRE 600 ribosomes. J Biol Chem. 1974 Jun 25;249(12):3808–3813. [PubMed] [Google Scholar]
  14. Noller H. F., Chang C., Thomas G., Aldridge J. Chemical modification of the transfer RNA and polyuridylic acid binding sites of Escherichia coli 30 s ribosomal subunits. J Mol Biol. 1971 Nov 14;61(3):669–679. doi: 10.1016/0022-2836(71)90071-4. [DOI] [PubMed] [Google Scholar]
  15. Peacock A. C., Dingman C. W. Molecular weight estimation and separation of ribonucleic acid by electrophoresis in agarose-acrylamide composite gels. Biochemistry. 1968 Feb;7(2):668–674. doi: 10.1021/bi00842a023. [DOI] [PubMed] [Google Scholar]
  16. Sanger F., Brownlee G. G., Barrell B. G. A two-dimensional fractionation procedure for radioactive nucleotides. J Mol Biol. 1965 Sep;13(2):373–398. doi: 10.1016/s0022-2836(65)80104-8. [DOI] [PubMed] [Google Scholar]
  17. Sawyer R. C., Dahlberg J. E. Small RNAs of Rous sarcoma virus: characterization by two-dimensional polyacrylamide gel electrophoresis and fingerprint analysis. J Virol. 1973 Dec;12(6):1226–1237. doi: 10.1128/jvi.12.6.1226-1237.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Shine J., Dalgarno L. Determinant of cistron specificity in bacterial ribosomes. Nature. 1975 Mar 6;254(5495):34–38. doi: 10.1038/254034a0. [DOI] [PubMed] [Google Scholar]
  19. Shine J., Dalgarno L. The 3'-terminal sequence of Escherichia coli 16S ribosomal RNA: complementarity to nonsense triplets and ribosome binding sites. Proc Natl Acad Sci U S A. 1974 Apr;71(4):1342–1346. doi: 10.1073/pnas.71.4.1342. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Szer W., Hermoso J. M., Leffler S. Ribosomal protein S1 and polypeptide chain initiation in bacteria. Proc Natl Acad Sci U S A. 1975 Jun;72(6):2325–2329. doi: 10.1073/pnas.72.6.2325. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Szer W., Leffler S. Interaction of Escherichia coli 30S ribosomal subunits with MS2 phage RNA in the absence of initiation factors. Proc Natl Acad Sci U S A. 1974 Sep;71(9):3611–3615. doi: 10.1073/pnas.71.9.3611. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Tal M., Aviram M., Kanarek A., Weiss A. Polyuridylic acid binding and translating by Escherichia coli ribosomes: stimulation by protein I, inhibition by aurintricarboxylic acid. Biochim Biophys Acta. 1972 Oct 27;281(3):381–392. doi: 10.1016/0005-2787(72)90452-2. [DOI] [PubMed] [Google Scholar]
  23. Van Dieijen G., Van Der Laken C. J., Van Knippenberg P. H., Van Duin J. Function of Escherichia coli ribosomal protein S1 in translation of natural and synthetic messenger RNA. J Mol Biol. 1975 Apr 15;93(3):351–366. doi: 10.1016/0022-2836(75)90282-x. [DOI] [PubMed] [Google Scholar]
  24. van Duin J., van Knippenberg P. H. Functional heterogeneity of the 30 S ribosomal subunit of Escherichia coli. 3. Requirement of protein S1 for translation. J Mol Biol. 1974 Mar 25;84(1):185–195. doi: 10.1016/0022-2836(74)90221-6. [DOI] [PubMed] [Google Scholar]
  25. van Knippenberg P. H., Hooykaas P. J., van Duin J. The stoichiometry of E. coli 30S ribosomal protein S1 on in vivo and in vitro polyribosomes. FEBS Lett. 1974 May 1;41(2):323–326. doi: 10.1016/0014-5793(74)81239-1. [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