Advertisement

Homologies Between Different Forms of 2-5A Synthetases

  • E. Truve
  • M. Kelve
  • A. Aaspollu
  • H. C. Schröder
  • W. E. G. Müller
Part of the Progress in Molecular and Subcellular Biology book series (PMSB, volume 14)

Abstract

(2′-5′) Oligoadenylate synthetases (2-5A synthetases; EC 2.7.7.19) are present in mammalian cells and tissues and synthesize from ATP a series of oligomers termed 2-5A [general formula: ppp(A2′p)nA; with 1 ≤ n < 18 and usually 1 ≤ n < 6] (Hovanessian 1991). For full enzymic activity of the 2-5A synthetases, binding of double-stranded RNA is required (Sen 1982). Three principal 2-5A synthetase isoenzymes have been described with Mr’s of 40–46, 69, and 100 kDa (Chebath et al. 1987; Hovanessian et al. 1987, 1988). In the following they are classified as 2-5A synthetase I [Mr 40–46 000], II [Mr 69 000] and III [Mr 100 000]. All three isoforms are induced in cells by interferon (Cohen et al. 1988; Rutherford et al. 1988). 2-5A synthetases I and II are present in both the nucleus and the mitochondria as well as in the rough/smooth microsomal fraction, while 2-5A synthetase III is associated with the rough microsomal fraction only (Hovanessian et al. 1987). The enzymic product, 2-5A, functions as an activator of the endoribonuclease L. 2-5A is rapidly degraded either by the relatively unspecific phosphodiesterase (Schmidt et al. 1979; Johnston and Hearl 1987) or the specific 2′,3′-exoribonuclease (Müller et al. 1980; Schröder et al. 1980, 1984).

Keywords

Synthetase Gene Ehrlich Ascites Tumor Cell Oligoadenylate Synthetase Protein Secondary Structure Prediction Helical Wheel 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Benech P, Mory Y, Revel M, Chebath J (1985) Structure of two forms of the interferon-induced (2′-5′) oligo A synthetase of human cells based on cDNAs and gene sequences. EMBO J 4:2249–2256.PubMedGoogle Scholar
  2. Chang CC, Wu JM (1991) Modulation of antiviral activity of intereferon and 2′,5′-oligoadenylate synthetase gene expression by mild hyperthermia (39.5°C) in cultured human cells. J Biol Chem 266:4605–4612.PubMedGoogle Scholar
  3. Chebath J, Benech P, Hovanessian A, Galabru J, Revel M (1987) Four different forms of interferon-induced 2′,5′-oligo(A) synthetase identified by immunoblotting in human cells. J Biol Chem 262:3852–3857.PubMedGoogle Scholar
  4. Coccia EM, Romeo G, Nissim A, Marziali G, Albertini R, Affabris E, Battistini A, Fiorucci G, Orsatti R, Rossi GB, Chebath J (1990) A full-length murine 2-5A synthetase cDNA transfected in NIH-3T3 cells impairs EMCV but not VSV replication. Virology 179:228–233.PubMedCrossRefGoogle Scholar
  5. Cohen B, Peretz D, Vaiman D, Benech P, Chebath J (1988) Enhancer-like interferon responsive sequences of the human and murine (2′-5′)oligoadenylate synthetase gene promotors. EMBO J 7:1411–1419.PubMedGoogle Scholar
  6. Gamier J, Osguthorpe DJ, Robson B (1978) Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. J Mol Biol 120:97–120.CrossRefGoogle Scholar
  7. Ghosh SK, Kusari J, Bandyopadhyay SK, Samanta H, Kumar R, Sen GC (1991) Cloning, sequencing, and expression of two murine 2′-5′-oligoadenylate synthetases: structure-function relationship. J Biol Chem 266:15293–15299.PubMedGoogle Scholar
  8. Hovanessian AG (1991) Interferon-induced and double-stranded RNA-activated enzymes: a specific protein kinase and 2′,5′-oligoadenylate synthetase. J Interferon Res 11:199–205.PubMedCrossRefGoogle Scholar
  9. Hovanessian AG, Laurent AG, Chebath J, Galabru J, Robert N, Svab J (1987) Identification of 69-kd and 100-kd forms of 2-5A-synthetase from interferon-treated human cells by specific monoclonal antibodies. EMBO J 5:1273–1280.Google Scholar
  10. Hovanessian AG, Svab J, Marié I, Robert N, Chamaret S, Laurent AG (1988) Characterization of 69-and 100-kDa forms of 2-5A-synthetase from interferon-treated human cells. J Biol Chem 263:4945–4949.PubMedGoogle Scholar
  11. Ichii Y, Fukunaga R, Shiojiri S, Sokawa Y (1986) Mouse 2-5A synthetase cDNA: nucleotide sequence and comparison to human 2-5A synthetase. Nucleic Acids Res 14:10117.PubMedCrossRefGoogle Scholar
  12. Johnston MI, Hearl WG (1987) Purification and characterization of a 2′-phosphodiesterase from bovine spleen. J Biol Chem 262:8377–8382.PubMedGoogle Scholar
  13. Kozak M (1984) Compilation analysis of sequences upstream from the translational start site in eukaryotic mRNAs. Nucleic Acids Res 12:857–872.PubMedCrossRefGoogle Scholar
  14. Laurent G St, Yoshie O, Floyd-Smith G, Samanta H, Sehgal PB (1983) Interferon action: two (2′-5′)(A)n synthetases specified by distinct mRNAs in Ehrlich ascites tumor cells treated with interferon. Cell 33:95–102.CrossRefGoogle Scholar
  15. Marié I, Hovanessian AG (1992) The 69-kDa 2-5A synthetase is composed of two homologous and adjacent functional domains. J Biol Chem 267:9933–9939.PubMedGoogle Scholar
  16. Moller W, Amons R (1985) Phosphate-binding sequences in nucleotide-binding proteins. FEBS Lett 186:1–7.PubMedCrossRefGoogle Scholar
  17. Müller WEG, Schröder HC, Zahn RK, Dose K (1980) Degradation of 2′,5′-linked oligoriboadenylates by 3′-exoribonuclease and 5′-nucleotidase. Hoppe-Seyler′s Z Physiol Chem 361:469–472.PubMedCrossRefGoogle Scholar
  18. PC/Gene (1991) User and reference manual; release 6.5. IntelliGenetics, Mountain View, CA 2,1991.Google Scholar
  19. Rutherford MN, Hannigan GE, Williams BRG (1988) Interferon-induced binding of nuclear factors to promoter elements of the 2-5A synthetase gene. EMBO J 7:751–759.PubMedGoogle Scholar
  20. Rutherford MN, Kumar A, Nissim A, Chebath J, Williams BRG (1991) The murine 2-5A synthetase locus: three distinct transcripts from two linked genes. Nucleic Acids Res 19:1917–1924.PubMedCrossRefGoogle Scholar
  21. Schmidt A, Chernajovsky Y, Shulman L, Federman P, Berissi H, Revel M (1979) An interferon-induced phosphodiesterase degrading (2′-5′)oligoadenylate and the C-C-A terminus of tRNA. Proc Natl Acad Sci USA 76:4788–4792.PubMedCrossRefGoogle Scholar
  22. Schröder HC, Zahn RK, Dose K, Müller WEG (1980) Purification and characterization of a poly (A)-specific exoribonuclease from calf thymus. J Biol Chem 255:4535–4538.PubMedGoogle Scholar
  23. Schröder HC, Gosselin G, Imbach J-L, Müller WEG (1984) Influence of the xyloadenosine analogue of 2′,5′-oligoriboadenylate degrading 2′,3′-exoribonuclease and further enzymes involved in poly(A) ( + )mRNA metabolism. Mol Biol Rep 10:83–89.PubMedCrossRefGoogle Scholar
  24. Schröder HC, Wenger R, Kuchino Y, Müller WEG (1989) Modulation of nuclear matrix-associated (2′-5′)oligoadenylate metabolism and ribonuclease L activity in H9 cells by human immunodeficiency virus. J Biol Chem 264:5669–5673.PubMedGoogle Scholar
  25. Sen GC (1982) Mechanism of interferon action: progress towards its understanding. Prog Nucleic Acid Res Mol Biol 27: 105–156.PubMedCrossRefGoogle Scholar
  26. Sinensky M, Lutz RJ (1992) The prenylation of proteins. Bioessays 14:25–31.PubMedCrossRefGoogle Scholar
  27. Wathelet M, Moutschen S, Cravador A, Dewit L, Defilippi P, Huez G, Content J (1986) Full-length sequence and expression of the 42 kDa 2-5A synthetase induced by human interferon. FEBS Lett 196:113–120.PubMedCrossRefGoogle Scholar
  28. Williams BRG, Silverman RH (eds) (1985) The 2-5A System. Liss, New York.Google Scholar
  29. Williams BRG, Golgher RR, Brown RE, Gilbert CS, Kerr IM (1979) Natural occurrence of 2-5A in interferon-treated EMC virus-infected L cells. Nature 282:582–586.PubMedCrossRefGoogle Scholar
  30. Zarkower D, Stephenson P, Sheets M, Wickens M (1986) The AAUAAA sequence is required both for cleavage and for polyadenylation of simian virus 40 pre-mRNA in vitro. Mol Cell Biol 6:2317–2323.PubMedGoogle Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 1994

Authors and Affiliations

  • E. Truve
    • 1
  • M. Kelve
    • 1
  • A. Aaspollu
    • 1
  • H. C. Schröder
    • 2
  • W. E. G. Müller
    • 2
  1. 1.Institute of Chemical Physics and BiophysicsTallinnEstonia
  2. 2.Institut für Physiologische Chemie, Abteilung Angewandte MolekularbiologieJohannes Gutenberg-UniversitätMainzGermany

Personalised recommendations