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U of T led research team uncovers evolutionary origins of prion disease gene
Date:9/28/2009

proteins contain extensive stretches of similar amino acid sequence. The researchers next documented that the respective segments within ZIP and prion proteins are computationally predicted to acquire a highly similar three-dimensional structure. Finally, the team uncovered multiple additional commonalities between ZIP and prion proteins which led them to conclude these molecules are evolutionarily related.

Most proteins do not act in isolation but partner with other proteins to exert their biological roles. The relationship between ZIP-family and prion proteins may thus provide a new angle from which to study the biology of the prion protein in health and disease. The level of shared characteristics between these protein families, in addition to the presence of prion protein genes in most chordate (i.e., backboned) species, place the split from the ZIP-like ancestor gene at the base of the chordate lineage.

Although no single evidence firmly established the phylogenetic relationship between ZIP and prion genes, Schmitt-Ulms is confident that the many corroborating pieces of evidence collected and, equally important, the absence of any conflicting observations, allow no other conclusion to be drawn.


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Contact: Jennifer Little
jennifer.little@utoronto.ca
416-946-8423
University of Toronto
Source:Eurekalert

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