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)


(2′-5′) Oligoadenylate synthetases (2-5A synthetases; EC 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).


Synthetase Gene Ehrlich Ascites Tumor Cell Oligoadenylate Synthetase Protein Secondary Structure Prediction Helical Wheel 
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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

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