Final Activity Report Summary - GWJ-NUI-MAY (Identification of potential prion proteins in plants)
The main aim of this project was to identify new prion proteins in plants. Recent work from various diverse species suggests that the term prion should not only be associated with diseases such as 'Mad cow disease' etc, but should be used as a general term for any protein that can behave in an infectious manner. This suggestion has far- reaching implications for many aspects of biological processes.
This project set out to apply what we know characterises a prion protein in Saccharomyces cerevisiae (baker's yeast) to try and identify potential prion- forming proteins in the model plant Arabidopsis thaliana. To this end we have identified two plant proteins that have the ability to form prions in a yeast system. The next and most challenging aspect is to establish whether these proteins can form prions in their natural environments. The pint must be emphasised, these potential prion proteins in plants are unrelated to human disease and potentially constitute a new mechanism in plants for altering protein function.
In addition to searching for new prion proteins, this project has also assessed the ability of plant chaperone proteins (to function correctly in yeast. A chaperone is a protein that helps other proteins to obtain their proper 3 dimensional structure- they are implicated in a number of human disease states) These experiments have helped address questions regarding the evolution of the Hsp70 protein (a major class of protein chaperone).
This project set out to apply what we know characterises a prion protein in Saccharomyces cerevisiae (baker's yeast) to try and identify potential prion- forming proteins in the model plant Arabidopsis thaliana. To this end we have identified two plant proteins that have the ability to form prions in a yeast system. The next and most challenging aspect is to establish whether these proteins can form prions in their natural environments. The pint must be emphasised, these potential prion proteins in plants are unrelated to human disease and potentially constitute a new mechanism in plants for altering protein function.
In addition to searching for new prion proteins, this project has also assessed the ability of plant chaperone proteins (to function correctly in yeast. A chaperone is a protein that helps other proteins to obtain their proper 3 dimensional structure- they are implicated in a number of human disease states) These experiments have helped address questions regarding the evolution of the Hsp70 protein (a major class of protein chaperone).