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Article

"Restoration" of glutathione transferase activity by single-site mutation of the yeast prion protein Ure2.

Journal of molecular biology - 19 Dec 2008

Zhang Zai-Rong, Bai Ming, Wang Xin-Yu, Zhou Jun-Mei, Perrett Sarah

Abstract excerpt

The yeast prion Ure2p is composed of an N-terminal prion domain, and a C-terminal globular domain, which shows similarity to glutathione transferases (GSTs) in both sequence and structure. Ure2p protects Saccharomyces cerevisiae cells from heavy metal ion and oxidant toxicity. Ure2p shows glutathione-dependent peroxidase (GPx) activity, which is often an adjunct activity of GSTs, but wild-type Ure2p shows no...

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Identifiers

PMID: 18845158
DOI: 10.1016/j.jmb.2008.09.047

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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"Restoration" of glutathione transferase activity by single-site mutation of the yeast prion protein Ure2.PMID 18845158Read ↗

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