SUP35/YDR172W Summary Help

Standard Name SUP35
Systematic Name YDR172W
Alias GST1 , PNM2 1 , SAL3 , SUF12 , SUP2 , SUP36
Feature Type ORF, Verified
Description Translation termination factor eRF3; has a role in mRNA deadenylation and decay; altered protein conformation creates the [PSI(+)] prion that alters translational fidelity and results in a nonsense suppressor phenotype (2, 3, 4, 5 and see Summary Paragraph)
Also known as: [PSI] , [PSI(+)]
Name Description SUPpressor
Gene Product Alias eRF3
Chromosomal Location
ChrIV:808324 to 810381 | ORF Map | GBrowse
Gbrowse
Genetic position: 142.87 cM
Gene Ontology Annotations All SUP35 GO evidence and references
  View Computational GO annotations for SUP35
Molecular Function
Manually curated
High-throughput
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 7 genes
Resources
Classical genetics
conditional
Large-scale survey
null
reduction of function
Resources
371 total interaction(s) for 235 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 59
  • Affinity Capture-RNA: 4
  • Affinity Capture-Western: 35
  • Biochemical Activity: 2
  • Co-crystal Structure: 5
  • Co-localization: 2
  • Co-purification: 2
  • Protein-peptide: 1
  • Reconstituted Complex: 41
  • Two-hybrid: 18

Genetic Interactions
  • Dosage Growth Defect: 1
  • Dosage Lethality: 7
  • Dosage Rescue: 9
  • Negative Genetic: 35
  • Phenotypic Enhancement: 9
  • Phenotypic Suppression: 42
  • Positive Genetic: 82
  • Synthetic Growth Defect: 6
  • Synthetic Lethality: 2
  • Synthetic Rescue: 9

Resources
Expression Summary
histogram
Resources
Length (a.a.) 685
Molecular Weight (Da) 76,551
Isoelectric Point (pI) 7
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrIV:808324 to 810381 | ORF Map | GBrowse
SGD ORF map
Genetic position: 142.87 cM
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..2058 808324..810381 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
Resources
External Links All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000002579
SUMMARY PARAGRAPH for SUP35

The [PSI+] prion determinant causes nonsense suppressor phenotype due to a reduced function of the translation termination factor Sup35p (eRF3) polymerized into amyloid fibrils. Prion state of the Rnq1 protein, [PIN+], is required for the [PSI+] de novo generation, but not propagation. Yeast [psi-] [PIN+] cells overproducing Sup35p can exhibit nonsense suppression without generation of a stable [PSI+]. In such cells most of Sup35p is present in amyloid polymers, though remaining Sup35p monomer is sufficient for normal translation termination. Presence of these polymers strictly depends on [PIN+], suggesting that their maintenance relies on efficient generation de novo, rather than inheritance. Sup35p polymers contain Rnq1p, confirming that Rnq1p polymers seed Sup35p polymerization (4).

Last updated: 2005-03-15 Contact SGD

References cited on this page View Complete Literature Guide for SUP35
1) Doel SM, et al.  (1994) The dominant PNM2- mutation which eliminates the psi factor of Saccharomyces cerevisiae is the result of a missense mutation in the SUP35 gene. Genetics 137(3):659-70
2) Lindquist S, et al.  (2001) Investigating protein conformation-based inheritance and disease in yeast. Philos Trans R Soc Lond B Biol Sci 356(1406):169-76
3) Derkatch IL, et al.  (2004) Effects of Q/N-rich, polyQ, and non-polyQ amyloids on the de novo formation of the [PSI+] prion in yeast and aggregation of Sup35 in vitro. Proc Natl Acad Sci U S A 101(35):12934-9
4) Salnikova AB, et al.  (2005) Nonsense suppression in yeast cells overproducing Sup35 (eRF3) is caused by its non-heritable amyloids. J Biol Chem 280(10):8808-12
5) Funakoshi Y, et al.  (2007) Mechanism of mRNA deadenylation: evidence for a molecular interplay between translation termination factor eRF3 and mRNA deadenylases. Genes Dev 21(23):3135-48