|Title||A candidate marsupial PrP gene reveals two domains conserved in mammalian PrP proteins.|
|Publication Type||Journal Article|
|Year of Publication||1995|
|Authors||Windl O, Dempster M, Estibeiro P, Lathe R|
|Date Published||1995 Jul 4|
|Keywords||Amino Acid Sequence, Animals, Base Sequence, Conserved Sequence, DNA, Antisense, Mammals, Marsupialia, Molecular Sequence Data, Open Reading Frames, Prions, Restriction Mapping, Sequence Analysis, DNA, Sequence Homology, Amino Acid, Species Specificity|
The normal function of the pathogenicity-related protein, PrP (or prion protein), is unknown. To shed light on functionally important domains, we have characterized a candidate marsupial PrP gene. The deduced marsupial PrP has an overall identity of about 80% to eutherian PrP at the amino acid (aa) level. This similarity is not equally distributed and two regions (aa 118-142 and 177-223) are particularly highly conserved. In contrast, a repeat region in the N-terminal half of the marsupial PrP shows dipeptide inserts not described in other PrP. Another particular feature of the marsupial gene is the lack of a continuous ORF on the antisense strand, as is found in most eutherian PrP. We propose that antisense ORFs found in other species are artefactual. Comparison with all known PrP argues that the molecule characterised is the true marsupial PrP orthologue.