Lian, Hui-Yong, Jiang, Yi, Zhang, Hong, Jones, Gary and Perrett, Sarah (2006) The yeast prion protein Ure2: Structure, function and folding. Biochimica et Biophysica Acta - Proteins and Proteomics, 1764 (3). pp. 535-545.
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Abstract
The Saccharomyces cerevisiae protein Ure2 functions as a regulator of nitrogen metabolism and as a glutathione-dependent peroxidase. Ure2 also has the characteristics of a prion, in that it can undergo a heritable conformational change to an aggregated state; the prion form of Ure2 loses the regulatory function, but the enzymatic function appears to be maintained. A number of factors are found to affect the prion properties of Ure2, including mutation and expression levels of molecular chaperones, and the effect of these factors on structure and stability are being investigated. The relationship between structure, function and folding for the yeast prion Ure2 are discussed.
Item Type: | Article |
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Keywords: | Prion; Amyloid; Glutathione transferase; Peroxidase; Protein Folding; Chaperone; |
Academic Unit: | Faculty of Science and Engineering > Biology |
Item ID: | 922 |
Depositing User: | Dr. Gary Jones |
Date Deposited: | 13 Mar 2008 |
Journal or Publication Title: | Biochimica et Biophysica Acta - Proteins and Proteomics |
Publisher: | Elsevier |
Refereed: | Yes |
Related URLs: | |
URI: | https://mural.maynoothuniversity.ie/id/eprint/922 |
Use Licence: | This item is available under a Creative Commons Attribution Non Commercial Share Alike Licence (CC BY-NC-SA). Details of this licence are available here |
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