Conformational change of glutathione-S-transferase by its co-expression with prion domain of yeast Ure2p |
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Authors: | LI Yunmin TIAN Bo RAO Zihe |
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Affiliation: | 1. Institute of Microbiology, Chinese Academy of Sciences, 2. Laboratory of Structure Biology, Tsinghua University, |
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Abstract: | The Ure2 protein from Saccharomyces cerevisisae has a changeable structure similar to that ofrnammalian prion protein. Its N-terminal is the prion domain (PrD) consisting of 65 amino acids which plays a critical role in yeast prion development. In this study, PrD gene was recombinated with glutathione-S-transferase(GST) gene, and a soluble GST-PrD(sGST-PrD) fusion protein was expressed in E. coli. sGST-PrD could spontaneously polymerize into amyloid fibrils in vitro, displaying typical β-sheet-type structure; it had increased resistance to proteinase K and exhibited amvloid-like optical properties. Moreover, the aggregated GST-PrD(aGST-PrD) could induce sGST-PrD to aggregate into fibrils. These results indicate that PrD could change the conformation of GST moiety in a recombinant protein with PrD to form a prion-like chimeric protein, which proves that PrD has the ability to mediate a prion-like conversion of other proteins fused with it. |
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Keywords: | yeast prion Ure2p prion domain(PrD) glutathione-S-transferase(GST) conformation |
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