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Ribonucleases and angiogenins from fish.

Elio Pizzo1, Pasquale Buonanno, Antimo Di Maro

  • 1Department of Structural and Functional Biology, University of Naples Federico II, Complesso M. S. Angelo, Via Cintia, 80126 Napoli, Italy.

The Journal of Biological Chemistry
|July 25, 2006
PubMed
Summary

Fish RNases, belonging to the vertebrate RNase superfamily, were isolated and characterized for the first time. These RNases exhibit low activity but possess angiogenic properties, suggesting they are ancestral to the superfamily.

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Area of Science:

  • Biochemistry
  • Evolutionary Biology
  • Molecular Biology

Background:

  • Ribonucleases (RNases) are crucial enzymes, but fish RNases have been elusive due to low activity and sequence divergence.
  • The RNase A superfamily, now termed the vertebrate RNase superfamily, includes diverse members with varying functions.

Purpose of the Study:

  • To isolate and characterize fish RNases for the first time.
  • To understand the evolutionary origins and functional properties of the vertebrate RNase superfamily.

Main Methods:

  • Isolation and characterization of fish RNases from Danio rerio (zebrafish).
  • Cloning and expression of fish RNase cDNAs and purification of recombinant proteins.
  • Functional assays for ribonucleolytic and angiogenic activity, phylogenetic analysis.

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Main Results:

  • Fish RNases were successfully isolated and characterized, confirming their place in the vertebrate RNase superfamily.
  • These RNases display very low RNA-degrading activity but possess angiogenic properties, comparable to mammalian angiogenins.
  • Phylogenetic analysis reveals these angiogenic fish RNases as the earliest diverging members of the superfamily.

Conclusions:

  • Angiogenic fish RNases represent the ancestral form of the vertebrate RNase superfamily.
  • The evolution of RNases likely progressed from angiogenic ancestors to diverse functional forms, including mammalian angiogenins and digestive RNases.