6533b7dafe1ef96bd126e248
RESEARCH PRODUCT
The (2'-5')Oligoadenylate Synthetase is Present in the Lowest Multicellular Organisms, the Marine Sponges. Demonstration of the Existence and Identification of its Reaction Products
Anne KuusksaluArno PihlakMerike KelveWerner E.g. Müllersubject
ReticulocytesBlotting WesternCross ReactionsIn Vitro TechniquesBiochemistrylaw.inventionMiceSpecies SpecificityWestern blotlawAdenine nucleotide2'5'-Oligoadenylate SynthetasemedicineAnimalsChromatography High Pressure LiquidProtein Synthesis InhibitorsAntiserumchemistry.chemical_classificationOligoribonucleotidesbiologymedicine.diagnostic_testAdenine Nucleotides2'-5'-OligoadenylateImmunochemistryBlood Proteinsbiology.organism_classificationBiological EvolutionMolecular biologyPoriferaRatsMolecular WeightSpongeEnzymeBiochemistrychemistryPolyclonal antibodiesbiology.proteinRecombinant DNARabbitsdescription
We have proved the presence of (2'-5')oligoadenylates [(2'-5')An] and oligoadenylate synthetase [(2'-5')An synthetase] in the marine sponge Geodia cydonium. (2'-5')An isolated from sponge crude extract competed with authentic (2'-5')An for binding to polyclonal antiserum against (2'-5')An. HPLC analysis revealed the presence of nucleotides eluting with molecular markers for (2'-5')A oligomers. The biological activity of sponge (2'-5')An was demonstrated by inhibiting the protein biosynthesis in rabbit reticulocyte lysate. The activity of the (2'-5')An synthetase, present in crude sponge extract, was found to be high compared to that in mammalian interferon-treated cell extract. The (2'-5')An synthetase from sponge extract binds to poly(I).poly(C) as does the mammalian enzyme. Western blot analysis with antibodies to recombinant rat 43-kDa (2'-5')An synthetase revealed in sponge immunologically related proteins with molecular masses of approximately 110, 65, 61 and 34 kDa. We conclude, that the (2'-5')An system has evolved from receptors and enzymes involved in cell adhesion and/or growth control.
year | journal | country | edition | language |
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1995-09-01 | European Journal of Biochemistry |