Loss of Octarepeats in Two Processed Prion Pseudogenes in the Red Squirrel, Sciurus vulgaris

O. Madsen, T.T. Kortum, H. Hupkes, W. Kohlen, T. Rheede, W.W. de Jong

Research output: Contribution to journalArticleAcademicpeer-review

Abstract

The N-terminal region of the mammalian prion protein (PrP) contains an 'octapeptide' repeat which is involved in copper binding. This eight- or nine-residue peptide is repeated four to seven times, depending on the species, and polymorphisms in repeat number do occur. Alleles with three repeats are very rare in humans and goats, and deduced PrP sequences with two repeats have only been reported in two lemur species and in the red squirrel, Sciurus vulgaris. We here describe that the red squirrel two-repeat PrP sequence actually represents a retroposed pseudogene, and that an additional and older processed pseudogene with three repeats also occurs in this species as well as in ground squirrels. We argue that repeat numbers may tend to contract rather than expand in prion retropseudogenes, and that functional prion genes with two repeats may not be viable
Original languageEnglish
Pages (from-to)356-363
JournalJournal of Molecular Evolution
Volume71
Issue number5-6
DOIs
Publication statusPublished - 2010

Keywords

  • creutzfeldt-jakob-disease
  • protein gene prnp
  • octapeptide repeats
  • binding
  • region
  • copper
  • prp
  • susceptibility
  • polymorphisms
  • deletion

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