ArticleGenetics2007
Importance of the Hsp70 ATPase domain in yeast prion propagation.
Article in Genetics, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 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
24 citing papers in PubMed, 37 citations in OpenAlex.
- Review
- Client processing is altered by novel myopathy-causing mutations in the HSP40 J domain.PloS one · 2020Article
- Not quite the SSAme: unique roles for the yeast cytosolic Hsp70s.Current genetics · 2019Review
- The β6/β7 region of the Hsp70 substrate-binding domain mediates heat-shock response and prion propagation.Cellular and molecular life sciences : CMLS · 2018Article
- Article
- Towards understanding the gliotoxin detoxification mechanism:Microbial cell (Graz, Austria) · 2016Article
- Review
- Deconstructing the genetic basis of spent sulphite liquor tolerance using deep sequencing of genome-shuffled yeast.Biotechnology for biofuels · 2015Article
- Global transcript and phenotypic analysis of yeast cells expressing Ssa1, Ssa2, Ssa3 or Ssa4 as sole source of cytosolic Hsp70-Ssa chaperone activity.BMC genomics · 2014Article
- Mutational analysis of Sse1 (Hsp110) suggests an integral role for this chaperone in yeast prion propagation in vivo.G3 (Bethesda, Md.) · 2013Article
- 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
- Using steered molecular dynamics to predict and assess Hsp70 substrate-binding domain mutants that alter prion propagation.PLoS computational biology · 2013Article
- Molecular characterization of an adaptive response to alkylating agents in the opportunistic pathogen Aspergillus fumigatus.Nucleic acids research · 2012Article
- Single methyl group determines prion propagation and protein degradation activities of yeast heat shock protein (Hsp)-70 chaperones Ssa1p and Ssa2p.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Article
- Self-protection against gliotoxin--a component of the gliotoxin biosynthetic cluster, GliT, completely protects Aspergillus fumigatus against exogenous gliotoxin.PLoS pathogens · 2010Article
- Structure and assembly properties of the N-terminal domain of the prion Ure2p in isolation and in its natural context.PloS one · 2010Article
- Loss of Hsp70 exacerbates pathogenesis but not levels of fibrillar aggregates in a mouse model of Huntington's disease.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2009Article
- Hsp70 structure, function, regulation and influence on yeast prions.Protein and peptide letters · 2009Review
- In vivo monitoring of the prion replication cycle reveals a critical role for Sis1 in delivering substrates to Hsp104.Molecular cell · 2008Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Saccharomyces cerevisiae non-Mendelian genetic element [PSI+] is the prion form of the translation termination factor Sup35p. The ability of [PSI+] to propagate efficiently has been shown previously to depend upon the action of protein chaperones. In this article we describe a genetic screen that identifies an array of mutants within the two major cytosolic Hsp70 chaperones of yeast, Ssa1p and Ssa2p, which impair the propagation of [PSI+]. All but one of the mutants was located within the ATPase domain of Hsp70, which highlights the important role of regulation of Hsp70-Ssa ATP hydrolysis in prion propagation. A subset of mutants is shown to alter Hsp70 function in a way that is distinct from that of previously characterized Hsp70 mutants that alter [PSI+] propagation and supports the importance of interdomain communication and Hsp70 interaction with nucleotide exchange factors in prion propagation. Analysis of the effects of Hsp70 mutants upon propagation of a second yeast prion [URE3] further classifies these mutants as having general or prion-specific inhibitory properties.
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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.