A new RNase sheds light on the RNase/angiogenin subfamily from zebrafish

Pizzo Elio , Antonello Merlino , Mimmo Turano , Irene Russo Krauss , Francesca Coscia , Anna Zanfardino , Mario Varcamonti , Adriana Furia , Concetta Giancola , Lelio Mazzarella , Filomena Sica , Giuseppe d'Alessio (1)

1 Dept of Structural and Functional Biology

Only recently extracellular RNases of the RNase A superfamily, with the characteristic CKxxNTF sequence signature, have been identified in fish. This has led to the recognition that these RNases are present in the whole vertebrate sub-phylum. In fact, they comprise the only enzyme family unique to vertebrates. Four RNases from zebrafish (Danio rerio) have been previously reported, with a very low RNase activity, some endowed, like human angiogenin, with powerful angiogenic and bactericidal activities. Here we report the three-dimensional structure, the thermodynamic behaviour, and the biological properties of a novel zebrafish RNase, ZF-RNase-5. The investigation of its structural and functional properties, extended to all other sub-family members, provides an inclusive description of the whole zebrafish RNase sub-family.

Mots clés: Life Sciences

Pizzo Elio, Antonello Merlino, Mimmo Turano, Irene Russo Krauss, Francesca Coscia, et al.. A new RNase sheds light on the RNase/angiogenin subfamily from zebrafish. Biochemical Journal, 2010, 433 (2), pp.345-355. ⟨10.1042/BJ20100892⟩. ⟨hal-00549894⟩