NDLI: Novel glutaredoxin activity of the yeast prion protein Ure2 reveals a native-like dimer within fibrils.

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Novel glutaredoxin activity of the yeast prion protein Ure2 reveals a native-like dimer within fibrils.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Zhang, Zai-rong Perrett, Sarah
Description	Author Affiliation: Zhang ZR ( National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang District, Beijing 100101, China.)
Abstract	Ure2 is the protein determinant of the Saccharomyces cerevisiae prion [URE3]. Ure2 has structural similarity to glutathione transferases, protects cells against heavy metal and oxidant toxicity in vivo, and shows glutathione-dependent peroxidase activity in vitro. Here we report that Ure2 (which has no cysteine residues) also shows thiol-disulfide oxidoreductase activity similar to that of glutaredoxin enzymes. This demonstrates that disulfide reductase activity can be independent of the classical glutaredoxin CXXC/CXXS motif or indeed an intrinsic catalytic cysteine residue. The kinetics of the glutaredoxin activity of Ure2 showed positive cooperativity for the substrate glutathione in both the soluble native state and in amyloid-like fibrils, indicating native-like dimeric structure within Ure2 fibrils. Characterization of the glutaredoxin activity of Ure2 sheds light on its ability to protect yeast from heavy metal ion and oxidant toxicity and suggests a role in reversible protein glutathionylation signal transduction. Observation of allosteric enzyme behavior within amyloid-like Ure2 fibrils not only provides insight into the molecular structure of the fibrils but also has implications for the mechanism of [URE3] prion formation.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	21
Volume Number	284
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2009-05-22
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Amyloid Metabolism Glutaredoxins Prions Protein Multimerization Saccharomyces Cerevisiae Proteins Saccharomyces Cerevisiae Enzymology Drug Effects Binding Sites Biocatalysis Cadmium Chloride Pharmacology Glutathione Glutathione Peroxidase Hydrogen Peroxide Insulin Kinetics Mutation Genetics Oxidation-Reduction Oxidoreductases Chemistry Protein Structure, Tertiary Reducing Agents Solubility Time Factors Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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