title: Zebrafish RNase T2 genes and the evolution of secretory ribonucleases in animals.
abstract: BACKGROUND
  Members of the Ribonuclease (RNase) T2 family are common models for enzymological studies, and their evolution has been well characterized in plants. This family of acidic RNases is widespread, with members in almost all organisms including plants, animals, fungi, bacteria and even some viruses. While several biological functions have been proposed for these enzymes in plants, their role in animals is unknown. Interestingly, in vertebrates most of the biological roles of plant RNase T2 proteins are carried out by members of a different family, RNase A. Still, RNase T2 proteins are conserved in these animals
  
  
  RESULTS
  As a first step to shed light on the role of animal RNase T2 enzymes, and to understand the evolution of these proteins while co-existing with the RNase A family, we characterized RNase Dre1 and RNase Dre2, the two RNase T2 genes present in the zebrafish (Danio rerio) genome. These genes are expressed in most tissues examined, including high expression in all stages of embryonic development, and their expression corresponds well with the presence of acidic RNase activities in every tissue analyzed. Embryo expression seems to be a conserved characteristic of members of this family, as other plant and animal RNase T2 genes show similar high expression during embryo development. While plant RNase T2 proteins and the vertebrate RNase A family show evidences of radiation and gene sorting, vertebrate RNase T2 proteins form a monophyletic group, but there is also another monophyletic group defining a fish-specific RNase T2 clade.
  
  
  CONCLUSIONS
  Based on gene expression and phylogenetic analyses we propose that RNase T2 enzymes carry out a housekeeping function. This conserved biological role probably kept RNase T2 enzymes in animal genomes in spite of the presence of RNases A. A hypothetical role during embryo development is also discussed.
authors.affiliation: Interdepartmental Genetics Graduate Program, Iowa State University, Ames, IA 50011, USA. mfeile@iastate.edu
authors.forename: Melissa S
authors.initials: MS
authors.lastname: Hillwig
authors.forename: Ludmila
authors.initials: L
authors.lastname: Rizhsky
authors.forename: Ying
authors.initials: Y
authors.lastname: Wang
authors.forename: Alisa
authors.initials: A
authors.lastname: Umanskaya
authors.forename: Jeffrey J
authors.initials: JJ
authors.lastname: Essner
authors.forename: Gustavo C
authors.initials: GC
authors.lastname: MacIntosh
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000235:genetics; D004625:Embryo, Nonmammalian / Q000378:metabolism; D004722:Endoribonucleases / Q000235:genetics*; D019143:Evolution, Molecular; D005260:Female; D029941:Fish Proteins / Q000235:genetics*; D015870:Gene Expression; D020869:Gene Expression Profiling; D008297:Male; D008969:Molecular Sequence Data; D010802:Phylogeny; D016415:Sequence Alignment; D017422:Sequence Analysis, DNA; D015027:Zebrafish / Q000235:genetics*
chemical_list: D018076:DNA, Complementary; D029941:Fish Proteins; D004722:Endoribonucleases; C022543:ribonuclease T(2)