ArticleThe Biochemical journal1999
Characterization of the interaction domains of Ure2p, a prion-like protein of yeast.
Article in The Biochemical journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
11 citing papers in PubMed.
- Extra N-terminal residues have a profound effect on the aggregation properties of the potential yeast prion protein Mca1.PloS one · 2010Article
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- The mechanisms of [URE3] prion elimination demonstrate that large aggregates of Ure2p are dead-end products.The EMBO journal · 2003Article
- Conservation of the prion properties of Ure2p through evolution.Molecular biology of the cell · 2003Article
- Conservation of a portion of the S. cerevisiae Ure2p prion domain that interacts with the full-length protein.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- The [URE3] phenotype: evidence for a soluble prion in yeast.EMBO reports · 2002Article
- Gln3p nuclear localization and interaction with Ure2p in Saccharomyces cerevisiae.The Journal of biological chemistry · 2001Article
- The crystal structure of the nitrogen regulation fragment of the yeast prion protein Ure2p.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- Prions in Saccharomyces and Podospora spp.: protein-based inheritance.Microbiology and molecular biology reviews : MMBR · 1999Review
- Two prion-inducing regions of Ure2p are nonoverlapping.Molecular and cellular biology · 1999Article
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In the yeast Saccharomyces cerevisiae, the non-Mendelian inherited genetic element [URE3] behaves as a prion. A hypothesis has been put forward which states that [URE3] arises spontaneously from its cellular isoform Ure2p (the product of the URE2 gene), and propagates through interactions of the N-terminal domain of the protein, thus leading to its aggregation and loss of function. In the present study, various N- and C-terminal deletion mutants of Ure2p were constructed and their cross-interactions were tested in vitro and in vivo using affinity binding and a two-hybrid analysis. We show that the self-interaction of the protein is mediated by at least two domains, corresponding to the first third of the protein (the so-called prion-forming domain) and the C-terminal catalytic domain.
Indexed as
Identifiers
10024516PMC1220066What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.