ArticleMolecular and cellular biology1999
Two prion-inducing regions of Ure2p are nonoverlapping.
Article in Molecular and cellular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 101 citations in OpenAlex.
- How Big Is the Yeast Prion Universe?International journal of molecular sciences · 2023Review
- Article
- The kinetics of TEM1 antibiotic degrading enzymes that are displayed on Ure2 protein nanofibrils in a flow reactor.PloS one · 2018Article
- Amino acid composition predicts prion activity.PLoS computational biology · 2017Article
- Yeast prions and human prion-like proteins: sequence features and prediction methods.Cellular and molecular life sciences : CMLS · 2014Review
- Extensive diversity of prion strains is defined by differential chaperone interactions and distinct amyloidogenic regions.PLoS genetics · 2014Article
- Alterations in the Ure2 αCap domain elicit different GATA factor responses to rapamycin treatment and nitrogen limitation.The Journal of biological chemistry · 2013Article
- Prions in yeast.Genetics · 2012Review
- Is tau ready for admission to the prion club?Prion · 2012Review
- Potential roles for prions and protein-only inheritance in cancer.Cancer metastasis reviews · 2012Review
- Article
- The mechanism of prion inhibition by HET-S.Molecular cell · 2010Article
- Structure and assembly properties of the N-terminal domain of the prion Ure2p in isolation and in its natural context.PloS one · 2010Article
- Distinct type of transmission barrier revealed by study of multiple prion determinants of Rnq1.PLoS genetics · 2010Article
- A promiscuous prion: efficient induction of [URE3] prion formation by heterologous prion domains.Genetics · 2009Article
- Moonlighting proteins in yeasts.Microbiology and molecular biology reviews : MMBR · 2008Review
- Propagation of the [PIN+] prion by fragments of Rnq1 fused to GFP.Current genetics · 2007Article
- Primary sequence independence for prion formation.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- Article
- In vivo specificity of Ure2 protection from heavy metal ion and oxidative cellular damage in Saccharomyces cerevisiae.Yeast (Chichester, England) · 2005Article
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2 authors at 1 institution in 1 country.
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Abstract
Ure2p of Saccharomyces cerevisiae normally functions in blocking utilization of a poor nitrogen source when a good nitrogen source is available. The non-Mendelian genetic element [URE3] is a prion (infectious protein) form of Ure2p, so that overexpression of Ure2p induces the de novo appearance of infectious [URE3]. Earlier studies defined a prion domain comprising Ure2p residues 1 to 64 and a nitrogen regulation domain included in residues 66 to 354. We find that deletion of individual runs of asparagine within the prion domain reduce prion-inducing activity. Although residues 1 to 64 are sufficient for prion induction, the fragment from residues 1 to 80 is a more efficient inducer of [URE3]. In-frame deletion of a region around residue 224 does not affect nitrogen regulation but does eliminate prion induction by the remainder of Ure2p. Larger deletions removing the region around residue 224 and more of the C-terminal part of Ure2p restore prion-inducing ability. A fragment of Ure2p lacking the original prion domain does not induce [URE3], but surprisingly, further deletion of residues 151 to 157 and 348 to 354 leaves a fragment that can do so. The region from 66 to 80 and the region around residue 224 are both necessary for this second prion-inducing activity. Thus, each of two nonoverlapping parts of Ure2p is sufficient to induce the appearance of the [URE3] prion.
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