Skip to main content
Nucleic Acids Research logoLink to Nucleic Acids Research
. 1994 Feb 11;22(3):321–324. doi: 10.1093/nar/22.3.321

The ribosomal RNA identity elements for ricin and for alpha-sarcin: mutations in the putative CG pair that closes a GAGA tetraloop.

A Glück 1, Y Endo 1, I G Wool 1
PMCID: PMC523583  PMID: 8127668

Abstract

alpha-Sarcin is a ribonuclease that cleaves the phosphodiester bond on the 3' side of G4325 in 28S rRNA; ricin A-chain is a RNA N-glycosidase that depurinates the 5' adjacent A4324. These single covalent modifications inactivate the ribosome. An oligoribonucleotide that reproduces the structure of the sarcin/ricin domain in 28S rRNA was synthesized and mutations were constructed in the 5' C and the 3' G that surround a GAGA tetrad that has the sites of toxin action. Covalent modification of the RNA by ricin, but not by alpha-sarcin, requires a Watson-Crick pair to shut off a putative GAGA tetraloop. Either the recognition elements for the two toxins are different despite their catalyzing covalent modification of adjacent nucleotides in 28S rRNA or there are transitions in the conformation of the alpha-sarcin/ricin domain in 28S rRNA and one conformer is recognized by alpha-sarcin and the other by ricin A-chain.

Full text

PDF
321

Images in this article

Selected References

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

  1. Endo Y., Chan Y. L., Lin A., Tsurugi K., Wool I. G. The cytotoxins alpha-sarcin and ricin retain their specificity when tested on a synthetic oligoribonucleotide (35-mer) that mimics a region of 28 S ribosomal ribonucleic acid. J Biol Chem. 1988 Jun 15;263(17):7917–7920. [PubMed] [Google Scholar]
  2. Endo Y., Glück A., Chan Y. L., Tsurugi K., Wool I. G. RNA-protein interaction. An analysis with RNA oligonucleotides of the recognition by alpha-sarcin of a ribosomal domain critical for function. J Biol Chem. 1990 Feb 5;265(4):2216–2222. [PubMed] [Google Scholar]
  3. Endo Y., Glück A., Wool I. G. Ribosomal RNA identity elements for ricin A-chain recognition and catalysis. J Mol Biol. 1991 Sep 5;221(1):193–207. doi: 10.1016/0022-2836(91)80214-f. [DOI] [PubMed] [Google Scholar]
  4. Endo Y., Tsurugi K. RNA N-glycosidase activity of ricin A-chain. Mechanism of action of the toxic lectin ricin on eukaryotic ribosomes. J Biol Chem. 1987 Jun 15;262(17):8128–8130. [PubMed] [Google Scholar]
  5. Endo Y., Tsurugi K. The RNA N-glycosidase activity of ricin A-chain. The characteristics of the enzymatic activity of ricin A-chain with ribosomes and with rRNA. J Biol Chem. 1988 Jun 25;263(18):8735–8739. [PubMed] [Google Scholar]
  6. Fernandez-Puentes C., Vazquez D. Effects of some proteins that inactivate the eukaryotic ribosome. FEBS Lett. 1977;78(1):143–146. doi: 10.1016/0014-5793(77)80292-5. [DOI] [PubMed] [Google Scholar]
  7. Glück A., Endo Y., Wool I. G. Ribosomal RNA identity elements for ricin A-chain recognition and catalysis. Analysis with tetraloop mutants. J Mol Biol. 1992 Jul 20;226(2):411–424. doi: 10.1016/0022-2836(92)90956-k. [DOI] [PubMed] [Google Scholar]
  8. Guillon J. M., Meinnel T., Mechulam Y., Lazennec C., Blanquet S., Fayat G. Nucleotides of tRNA governing the specificity of Escherichia coli methionyl-tRNA(fMet) formyltransferase. J Mol Biol. 1992 Mar 20;224(2):359–367. doi: 10.1016/0022-2836(92)91000-f. [DOI] [PubMed] [Google Scholar]
  9. Hausner T. P., Atmadja J., Nierhaus K. H. Evidence that the G2661 region of 23S rRNA is located at the ribosomal binding sites of both elongation factors. Biochimie. 1987 Sep;69(9):911–923. doi: 10.1016/0300-9084(87)90225-2. [DOI] [PubMed] [Google Scholar]
  10. Lee C. P., Seong B. L., RajBhandary U. L. Structural and sequence elements important for recognition of Escherichia coli formylmethionine tRNA by methionyl-tRNA transformylase are clustered in the acceptor stem. J Biol Chem. 1991 Sep 25;266(27):18012–18017. [PubMed] [Google Scholar]
  11. Moazed D., Robertson J. M., Noller H. F. Interaction of elongation factors EF-G and EF-Tu with a conserved loop in 23S RNA. Nature. 1988 Jul 28;334(6180):362–364. doi: 10.1038/334362a0. [DOI] [PubMed] [Google Scholar]
  12. Montanaro L., Sperti S., Mattioli A., Testoni G., Stirpe F. Inhibition by ricin of protein synthesis in vitro. Inhibition of the binding of elongation factor 2 and of adenosine diphosphate-ribosylated elongation factor 2 to ribosomes. Biochem J. 1975 Jan;146(1):127–131. doi: 10.1042/bj1460127. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Szewczak A. A., Chan Y. L., Moore P. B., Wool I. G. On the conformation of the alpha sarcin stem-loop of 28S rRNA. Biochimie. 1991 Jul-Aug;73(7-8):871–877. doi: 10.1016/0300-9084(91)90128-n. [DOI] [PubMed] [Google Scholar]
  14. Woese C. R., Winker S., Gutell R. R. Architecture of ribosomal RNA: constraints on the sequence of "tetra-loops". Proc Natl Acad Sci U S A. 1990 Nov;87(21):8467–8471. doi: 10.1073/pnas.87.21.8467. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Wool I. G., Glück A., Endo Y. Ribotoxin recognition of ribosomal RNA and a proposal for the mechanism of translocation. Trends Biochem Sci. 1992 Jul;17(7):266–269. doi: 10.1016/0968-0004(92)90407-z. [DOI] [PubMed] [Google Scholar]

Articles from Nucleic Acids Research are provided here courtesy of Oxford University Press

RESOURCES