Identification of a novel member of 2H phosphoesterases, 2',5'-oligoadenylate degrading ribonuclease from the oyster Crassostrea gigas.

Item request has been placed! ×
Item request cannot be made. ×
loading   Processing Request
Read More Add to Saved list
  • Additional Information
    • Source:
      Publisher: Editions Scientifiques Elsevier Country of Publication: France NLM ID: 1264604 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1638-6183 (Electronic) Linking ISSN: 03009084 NLM ISO Abbreviation: Biochimie Subsets: MEDLINE
    • Publication Information:
      Publication: Paris : Editions Scientifiques Elsevier
      Original Publication: Paris.
    • Subject Terms:
      Adenine Nucleotides*/chemistry ; Adenine Nucleotides*/metabolism ; Oligoribonucleotides*/chemistry ; Oligoribonucleotides*/metabolism ; Ribonucleases*/chemistry ; Ribonucleases*/metabolism; Crassostrea/*enzymology; Animals ; Catalysis ; Substrate Specificity/physiology
    • Abstract:
      Several genes of IFN-mediated pathways in vertebrates, among them the genes that participate in the 2',5'-oligoadenylate synthetase (OAS)/RNase L pathway, have been identified in C. gigas. In the present study, we identified genes, which encode proteins having 2',5'-oligoadenylate degrading activity in C. gigas. These proteins belong to the 2H phosphoesterase superfamily and have sequence similarity to the mammalian A kinase anchoring protein 7 (AKAP7) central domain, which is responsible for the 2',5'-phosphodiesterase (2',5'-PDE) activity. Comparison of the genomic structures of C. gigas proteins with that of AKAP7 suggests that these enzymes originate from a direct common ancestor. However, the identified nucleases are not typical 2',5'-PDEs. The found enzymes catalyse the degradation of 2',5'-linked oligoadenylates in a metal-ion-independent way, yielding products with 2',3' -cyclic phosphate and 5'-OH termini similarly to the 3'-5' bond cleavage in RNA, catalyzed by metal-independent ribonucleases. 3',5'-linked oligoadenylates are not substrates for them. The preferred substrates for the C. gigas enzymes are 5'-triphosphorylated 2',5'-oligoadenylates, whose major cleavage reaction results in the removal of the 5'-triphosphorylated 2',3'-cyclic phosphate derivative, leaving behind the respective unphosphorylated 2',5'-oligoadenylate. Such a cleavage reaction results in the direct inactivation of the biologically active 2-5A molecule. The 2',5'-ribonucleases (2',5'-RNases) from C. gigas could be members of the ancient group of ribonucleases, specific to 2'-5' phosphodiester bond, together with the enzyme that was characterized previously from the marine sponge Tethya aurantium. The novel 2',5'-RNases may play a role in the control of cellular 2-5A levels, thereby limiting damage to host cells after viral infection.
      (Copyright © 2018. Published by Elsevier B.V.)
    • Contributed Indexing:
      Keywords: 2H phosphoesterases; 2–5A degradation; 2′,5′-ribonuclease; AKAP7; Crassostrea gigas
    • Accession Number:
      0 (Adenine Nucleotides)
      0 (Oligoribonucleotides)
      61172-40-5 (2',5'-oligoadenylate)
      EC 3.1.- (Ribonucleases)
    • Publication Date:
      Date Created: 20180909 Date Completed: 20190109 Latest Revision: 20190109
    • Publication Date:
      20221213
    • Accession Number:
      10.1016/j.biochi.2018.09.003
    • Accession Number:
      30195052