PUBLICATION

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

Authors
Pizzo, E., Merlino, A., Turano, M., Russo Krauss, I., Coscia, F., Zanfardino, A., Varcamonti, M., Furia, A., Giancola, C., Mazzarella, L., Sica, F., and D'Alessio, G.
ID
ZDB-PUB-101108-33
Date
2011
Source
The Biochemical journal   433(2): 345-355 (Journal)
Registered Authors
Keywords
none
MeSH Terms
  • Amino Acid Sequence
  • Animals
  • Cells, Cultured
  • Gene Expression Regulation, Developmental
  • Gene Expression Regulation, Enzymologic
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Structure, Tertiary
  • Ribonuclease, Pancreatic/chemistry*
  • Ribonuclease, Pancreatic/genetics
  • Ribonuclease, Pancreatic/metabolism
  • Ribonucleases/chemistry*
  • Ribonucleases/genetics
  • Ribonucleases/metabolism
  • Sequence Alignment
  • Zebrafish/embryology
  • Zebrafish/genetics
  • Zebrafish/metabolism*
PubMed
21050179 Full text @ Biochem. J.
Abstract
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.
Genes / Markers
Figures
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Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Antibodies
Orthology
Engineered Foreign Genes
Mapping