ArticleProceedings of the National Academy of Sciences of the United States of America2001
The crystal structure of the nitrogen regulation fragment of the yeast prion protein Ure2p.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 98 citations in OpenAlex.
- A Gene fromJournal of fungi (Basel, Switzerland) · 2023Article
- Structural and Mechanistic Insights into C-S Bond Formation in Gliotoxin.Angewandte Chemie (International ed. in English) · 2021Article
- Mutations Outside the Ure2 Amyloid-Forming Region Disrupt [URE3] Prion Propagation and Alter Interactions with Protein Quality Control Factors.Molecular and cellular biology · 2020Article
- Spin Label Scanning Reveals Likely Locations of β-Strands in the Amyloid Fibrils of the Ure2 Prion Domain.ACS omega · 2020Article
- Direct Observation of Oligomerization by Single Molecule Fluorescence Reveals a Multistep Aggregation Mechanism for the Yeast Prion Protein Ure2.Journal of the American Chemical Society · 2018Article
- Article
- Human J-protein DnaJB6b Cures a Subset of Saccharomyces cerevisiae Prions and Selectively Blocks Assembly of Structurally Related Amyloids.The Journal of biological chemistry · 2016Article
- Self-Assembly of Amyloid Fibrils That Display Active Enzymes.ChemCatChem · 2014Article
- Network-dosage compensation topologies as recurrent network motifs in natural gene networks.BMC systems biology · 2014Article
- Influence of specific HSP70 domains on fibril formation of the yeast prion protein Ure2.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2013Article
- Alterations in the Ure2 αCap domain elicit different GATA factor responses to rapamycin treatment and nitrogen limitation.The Journal of biological chemistry · 2013Article
- Identification of a small molecule that modifies MglA/SspA interaction and impairs intramacrophage survival of Francisella tularensis.PloS one · 2013Article
- Prions in yeast.Genetics · 2012Review
- Prion domain of yeast Ure2 protein adopts a completely disordered structure: a solid-support EPR study.PloS one · 2012Article
- Characterization of an Nmr homolog that modulates GATA factor-mediated nitrogen metabolite repression in Cryptococcus neoformans.PloS one · 2012Article
- Hierarchical organization in the amyloid core of yeast prion protein Ure2.The Journal of biological chemistry · 2011Article
- The core of Ure2p prion fibrils is formed by the N-terminal segment in a parallel cross-β structure: evidence from solid-state NMR.Journal of molecular biology · 2011Article
- In Sup35p filaments (the [PSI+] prion), the globular C-terminal domains are widely offset from the amyloid fibril backbone.Molecular microbiology · 2011Article
- Amyloid-like aggregates of the yeast prion protein ure2 enter vertebrate cells by specific endocytotic pathways and induce apoptosis.PloS one · 2010Article
- Disulfide bond formation significantly accelerates the assembly of Ure2p fibrils because of the proximity of a potential amyloid stretch.The Journal of biological chemistry · 2009Article
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Authors and funding
5 authors at 1 institution in 1 country.
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Abstract
The yeast nonchromosomal gene [URE3] is due to a prion form of the nitrogen regulatory protein Ure2p. It is a negative regulator of nitrogen catabolism and acts by inhibiting the transcription factor Gln3p. Ure2p residues 1--80 are necessary for prion generation and propagation. The C-terminal fragment retains nitrogen regulatory activity, albeit somewhat less efficiently than the full-length protein, and it also lowers the frequency of prion generation. The crystal structure of this C-terminal fragment, Ure2p(97--354), at 2.3 A resolution is described here. It adopts the same fold as the glutathione S-transferase superfamily, consistent with their sequence similarity. However, Ure2p(97--354) lacks a properly positioned catalytic residue that is required for S-transferase activity. Residues within this regulatory fragment that have been indicated by mutational studies to influence prion generation have been mapped onto the three-dimensional structure, and possible implications for prion activity are discussed.
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