Mammalian Genome

, 20:749

RNase 1 genes from the family Sciuridae define a novel rodent ribonuclease cluster

Authors

  • Steven J. Siegel
    • Laboratory of Allergic DiseasesNational Institute of Allergy and Infectious Diseases, National Institutes of Health
  • Caroline M. Percopo
    • Laboratory of Allergic DiseasesNational Institute of Allergy and Infectious Diseases, National Institutes of Health
  • Kimberly D. Dyer
    • Laboratory of Allergic DiseasesNational Institute of Allergy and Infectious Diseases, National Institutes of Health
  • Wei Zhao
    • Laboratory of Allergic DiseasesNational Institute of Allergy and Infectious Diseases, National Institutes of Health
    • Biochemical Engineering CollegeBeijing Union University
  • V. Louise Roth
    • Biology DepartmentDuke University
  • John M. Mercer
    • Biology DepartmentDuke University
    • Laboratory of Allergic DiseasesNIAID, NIH
Article

DOI: 10.1007/s00335-009-9215-4

Cite this article as:
Siegel, S.J., Percopo, C.M., Dyer, K.D. et al. Mamm Genome (2009) 20: 749. doi:10.1007/s00335-009-9215-4

Abstract

The RNase A ribonucleases are a complex group of functionally diverse secretory proteins with conserved enzymatic activity. We have identified novel RNase 1 genes from four species of squirrel (order Rodentia, family Sciuridae). Squirrel RNase 1 genes encode typical RNase A ribonucleases, each with eight cysteines, a conserved CKXXNTF signature motif, and a canonical His12-Lys41-His119 catalytic triad. Two alleles encode Callosciurus prevostii RNase 1, which include a Ser18↔Pro, analogous to the sequence polymorphisms found among the RNase 1 duplications in the genome of Rattus exulans. Interestingly, although the squirrel RNase 1 genes are closely related to one another (77–95% amino acid sequence identity), the cluster as a whole is distinct and divergent from the clusters including RNase 1 genes from other rodent species. We examined the specific sites at which Sciuridae RNase 1s diverge from Muridae/Cricetidae RNase 1s and determined that the divergent sites are located on the external surface, with complete sparing of the catalytic crevice. The full significance of these findings awaits a more complete understanding of biological role of mammalian RNase 1s.

Copyright information

© US Government 2009