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.
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This work was supported by NIAID DIR funding to HFR and National Science Foundation #DEB 9726855 to JMM and VLR.
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Steven J. Siegel and Caroline M. Percopo contributed equally to this work.
Sequence data from this article have been deposited with the DDBJ/EMBL/GenBank Data Libraries under Accession Nos. FJ659109 – FJ659113.
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Siegel, S.J., Percopo, C.M., Dyer, K.D. et al. RNase 1 genes from the family Sciuridae define a novel rodent ribonuclease cluster. Mamm Genome 20, 749–757 (2009). https://doi.org/10.1007/s00335-009-9215-4
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DOI: https://doi.org/10.1007/s00335-009-9215-4