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At high concentrations, Hsp104 eliminates Sup35 prions. Paper-13049537.
Interactions of the chaperone Hsp104 with yeast Sup35 and mammalian PrP. Paper-1267127.
Similarly to Sup35p, in [ PSI+] cells Sup45p was found in aggregates. Paper-984099.
Hsp104 binds to yeast Sup35 prion fiber but needs other factor(s) to sever it. Paper-10872818.
SUP35 and SUP45 genes determine the accuracy of translation at the stage of termination. Paper-631504.
Overexpression of Sup45p, but not other tested essential Sup35p binding partners, caused rescue. Paper-14004898.
The presence of pseudoknots in yeast Sup35p and Rnq1 suggests acquisition in the prokaryotic era. Paper-8733401.
These data are consistent with Sup35p and Sup45p forming a complex with release factor properties. Paper-360996.
Pathogenic polyglutamine tracts are potent inducers of spontaneous Sup35 and Rnq1 amyloidogenesis. Paper-14274732.
Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers. Paper-10211370.
Suppression induced by extra- SUP35 and especially by extra- SUP45 is affected by the cell environment. Paper-69716.
Hsp104, Hsp70 and Hsp40 interplay regulates formation, growth and elimination of Sup35 prions. Paper-13049537.
Importance of low-oligomeric-weight species for prion propagation in the yeast prion system Sup35/ Hsp104. Paper-9948275.
The yeast prions [URE3] and [ PSI(+)] are self-propagating amyloids of Ure2p and Sup35p, respectively. Paper-12346114.
The interaction of Hsp104 with yeast prion fibers made of Sup35NM, a prion-inducing domain of Sup35, was tested. Paper-10872818.
In contrast, Ssa1p together with either of its Hsp40 cochaperones blocks Sup35p polymerization. Paper-11376069.
We show that Hsp104p greatly stimulates the assembly of Sup35p into fibrils, whereas Ydj1p has inhibitory effect. Paper-11376069.
Increased [ PSI+] appearance by fusion of Rnq1 with the prion domain of Sup35 in Saccharomyces cerevisiae. Paper-13881558.
A multicopy plasmid carrying the wild-type SUP35 gene enhanced the efficiency of sup111 in psi- cytoplasm. Paper-38504.
We find here that Dcp1p can interact with the release factor eRF3p ( Sup35p) in Saccharomyces cerevisiae. Paper-11832159.
Sensitivity of sup35 and sup45 suppressor mutants in Saccharomyces cerevisiae to the anti-microtubule drug benomyl. Paper-631504.
These data are consistent with a model of [ PSI+] induction caused by physical interactions between Rnq1p and Sup35p. Paper-13732991.
Despite retention of [ PSI(+)], excess Hsp104 decreases toxicity of overproduced Sup35 in [ PSI(+)] strains. Paper-11366278.
Furthermore, it suggests that [RNQ(+)] requires less Hsp104p activity to maintain transmissible protein aggregates than Sup35p. Paper-14068554.
The SUP45 and SUP35 genes of Saccharomyces cerevisiae encode polypeptide chain release factors eRF1 and eRF3, respectively. Paper-984099.
Chromosome stability in suppressor mutants for SUP35 and SUP45 genes coding for translation release factors was studied. Paper-8439427.
The products of the SUP45 ( eRF1) and SUP35 genes interact to mediate translation termination in Saccharomyces cerevisiae. Paper-360996.
The inheritance of [ PSI+] and the physical state of Sup35 in vivo depend on the protein chaperone Hsp104 (heat shock protein 104). Paper-1267127.
Interaction between yeast Sup45p (eRF1) and Sup35p (eRF3) polypeptide chain release factors: implications for prion-dependent regulation. Paper-984099.
Experiments with RNA isolated from yeast mutant with impaired splicing demonstrated that sup1 and sup2 genes do not contain introns. Paper-5164560.
Absence of structural homology between sup1 and sup2 genes of yeast Saccharomyces cerevisiae and identification of their transcripts. Paper-5164560.
By Northern blotting analysis the sizes of the transcripts were determined to be 1.6 kb for sup1 gene and 2.5 and 1.4kb for sup2 gene. Paper-5164560.
Here, we report how the Ssa and Ssb components of the Hsp70 chaperone system directly affect Sup35 prionogenesis and cooperate with Hsp104. Paper-13049537.
The [URE3] and [ PSI (+)] prions of Saccharomyces cerevisiae are self-propagating amyloid forms of Ure2p and Sup35p, respectively. Paper-14380363.
The [URE3] and [ PSI+] prions of Saccharomyces cerevisiae are infectious amyloid forms of the proteins Ure2p and Sup35p, respectively. Paper-11023974.
A majority of sup35 and sup45 suppressor mutations confer supersensitivity to benomyl, the drug which de-polymerizes microtubules. Paper-631504.
The direct hybridization of DNA fragments, containing cloned sup1 and sup2 genes, did not reveal any structural homology between these two genes. Paper-5164560.
Overexpression of the SUP45 gene encoding a Sup35p-binding protein inhibits the induction of the de novo appearance of the [ PSI+] prion. Paper-1363853.
Two sites for Sup45p binding were found within Sup35p: one is formed by the N and M domains, and the other is located within the C domain. Paper-984099.
We also show that SUP45 overexpression counteracts the growth inhibition usually associated with overexpression of SUP35 in [ PSI+] strains. Paper-1363853.
Recessive mutations in SUP35 and SUP45 genes coding for translation release factors affect chromosome stability in Saccharomyces cerevisiae. Paper-8439427.
We used prion-forming domains from two budding yeast proteins ( Sup35p and New1p) to examine the requirements for prion formation and inheritance. Paper-10549352.
We show, using the two-hybrid system, that in Saccharomyces cerevisiae Sup45p and the product of the SUP35 gene ( Sup35p) interact in vivo. Paper-360996.
These genes act as dosage suppressors of a synthetic growth defect caused by some mutations in the SUP45 and SUP35 genes encoding eRF1 and eRF3, respectively. Paper-13871745.
The ability of Sup45p C-terminally tagged with (His)6 to specifically precipitate Sup35p from a cell lysate was used to confirm this interaction in vitro. Paper-360996.
This suggests [ PSI(+)] toxicity caused by excess Sup35p verses Sup35NMp is, respectively, through sequestration/inactivation of Sup45p verses Sup35p. Paper-14004898.
Deletion of the gene coding for the actin assembly protein Sla2 is lethal in cells containing the prion isoforms of both Sup35 and Rnq1 proteins simultaneously. Paper-10841034.
Furthermore, Ssa1p and Ydj1p or Sis1p can counteract the stimulatory activity of Hsp104p, by forming complexes with Sup35p oligomers, in an ATP-dependent manner. Paper-11376069.
Ure2p and Sup35p, two yeast prion proteins, can still form prions when the prion domains are shuffled, indicating a parallel in-register beta-sheet structure. Paper-11449429.
The N domain of Sup35p, responsible for its aggregation in [ PSI+] cells, may thus act as a repressor of another polypeptide chain release factor, Sup45p. Paper-984099.
The Hsp40 chaperones, Sis1 and Ydj1, preferentially interact with Sup35 oligomers and fibres compared with monomers, and facilitate Ssa1 and Ssb1 binding. Paper-13049537.
Thus, it appears that ERFs exert their regulatory functions in different ways, with ERF2 and ERF4 being activators and ERF3 being a repressor of transcription. Paper-8445254.
Ure2, Sup35 and Rnq1 in Saccharomyces cerevisiae and HET-s in Podospora anserina have been genetically and biochemically identified as prion proteins. Paper-14278916.
If cross-seeding events take place in the cytoplasm of yeast cells, the collision frequency between Rnq1 aggregates and Sup35 will affect the appearance of [ PSI(+)]. Paper-13881558.
Tethered poly(A)-binding protein ( Pab1p), used as a mimic of a normal 3'-UTR, recruits the termination factor Sup35p (eRF3) and stabilizes nonsense-containing mRNAs. Paper-10859064.
It is known that combination of [ PSI(+)] with some mutant alleles of the SUP35 or SUP45 genes in one and the same haploid yeast cell causes synthetic lethality. Paper-14278924.
Here we showed that aggregates made by overexpression of two different prion domains of Sup35 and Rnq1, were stained in yeast by thioflavin-S, an amyloid binding compound. Paper-9967860.
In contrast to ERF2 and ERF4, ERF3 reduced the transcription of the reporter gene in tobacco protoplasts, indicating that ERF3 functions as a repressor. Paper-8445254.
The aggregation of Sup45p is caused by its binding to Sup35p and was not observed when the aggregated Sup35p fragments did not contain sites for Sup45p binding. Paper-984099.
Genetic study of interactions between the cytoskeletal assembly protein sla1 and prion-forming domain of the release factor Sup35 (eRF3) in Saccharomyces cerevisiae. Paper-8297314.
Formation of the first structure requires the 48S ribosomal complex, whereas the second requires an 80S ribosome and the termination factors eRF3/ Sup35 and eRF1/ Sup45. Paper-12852927.
The protein-remodeling factor Hsp104 governs inheritance of [ PSI+], a yeast prion formed by self-perpetuating amyloid conformers of the translation termination factor Sup35. Paper-10211370.
To explain the [RNQ(+)] effect on the appearance of [ PSI(+)], the cross-seeding model was suggested, in which Rnq1 aggregates act as imperfect templates for Sup35 aggregation. Paper-13881558.
Furthermore, overexpression of either Xenopus or human eRF1 ( SUP45) genes also resulted in anti-suppression only if that strain was also overexpressing the yeast SUP35 gene. Paper-360996.
Taking into account the fact that Hsp104 is required for maintenance of [ PSI+], we suggest that low-oligomeric-weight species of Sup35 are important for prion propagation in yeast. Paper-9948275.
Extra copies of TEF5 and TEF3 can also suppress the temperature sensitivity of some sup45 and sup35 mutants and reduce nonsense codon readthrough caused by these omnipotent suppressors. Paper-13871745.
We obtained spontaneous and UV-induced sup35 or sup45 mutants in a haploid strain disomic for chromosome III and tested the stability of an extra copy of this chromosome. Paper-8439427.
This study supports the occurrence of in vivo cross-seeding between Sup35 and Rnq1 and provides a new tool that can be used to dissect the mechanism of the de novo appearance of prions. Paper-13881558.
In yeast Saccharomyces cerevisiae translation termination factors eRF1 ( Sup45) and eRF3 ( Sup35) are encoded by the essential genes SUP45 and SUP35 respectively. Paper-14278924.
In this study, to address whether cross-seeding occurs in vivo, a new [ PSI(+)] induction method was developed that exploits a protein fusion between the prion domain of Sup35 (NM) and Rnq1. Paper-13881558.
The shuffleability of a prion domain further suggests that the beta-sheet structure is of the parallel in-register type, and indeed, the normal Ure2 and Sup35 prion domains have such a structure. Paper-14380363.
Hsp104, Sis1, and Sse1 interact preferentially with the prion versus nonprion form of Sup35, whereas Sla2 and Ssb1/2 interact with both forms of Sup35 with similar efficiency. Paper-14327972.
The suppressors that act recessively upon these markers fell into two complementation groups; the sup47 and sup36 suppressors show linkage to the tyr1 locus and the aro1 locus, respectively. Paper-14807108.
We confirmed that a genetic interaction exists between eRF3 and Pab1p and showed that Pab1p overexpression enhances the efficiency of termination in SUP35 (eRF3) mutant and [ PSI(+)] cells. Paper-9205566.
The [ PSI(+)] and [PIN(+)] prion-forming proteins are, respectively, the translational termination factor Sup35 and the yet poorly characterized Rnq1 protein that is rich in glutamines and asparagines. Paper-12424807.
We demonstrate that two shuffled Ure2 prion domains capable of being prions form parallel in-register beta-sheet structures, and our data indicate the same conclusion for a single shuffled Sup35 prion domain. Paper-14380363.
We now show that SUP45 overexpression inhibits the induction of [ PSI+] by Sup35p overproduction in [PIN+] strains, but has no effect on the propagation of [ PSI+] or on the [PIN] status of the cells. Paper-1363853.
In a Sla1(-) background, [ PSI] curing by dimethylsulfoxide or excess Hsp104 is increased, while translational readthrough and de novo [ PSI] formation induced by excess Sup35 or Sup35N are decreased. Paper-8297314.
We observe in vitro that addition of catalytic amounts of Hsp104 to the prion-determining region of the NM domain of Sup35, Sup355-26, results in the dissociation of oligomeric Sup35 into monomeric species. Paper-9948275.
However, as Tuite discusses in his Perspective, the Sup35p and Ure2p proteins of yeast that exist in both normal and infectious forms are providing evidence that the "protein-only" hypothesis may be right (Sparrer et al.). Paper-8477908.
Because Sup45p complexes with Sup35p, we hypothesize that excess Sup45p may sequester Sup35p, thereby reducing the opportunity for Sup35p conformational flips and/or self-interactions leading to prion formation. Paper-1363853.
We report that when purified Sup35 and Hsp104 are mixed, the circular dichroism (CD) spectrum differs from that predicted by the addition of the proteins' individual spectra, and the ATPase activity of Hsp104 is inhibited. Paper-1267127.
Through co-immunoprecipitation experiments, we show that Rli1 interacts physically with the translation termination factors eukaryotic release factor 1 (eRF1)/Sup45 and eRF3/ Sup35 in Saccharomyces cerevisiae. Paper-14185409.
Remarkably, the production of Sup35C in a sup45 mutant strain is also accompanied by an increase in the Sup45 levels, suggesting that translationally active Sup35 up-regulates Sup45 or protects it from degradation. Paper-14278924.
In contrast, [ PSI(+)] toxicity caused by a high excess of the Sup35p prion domain (Sup35NMp) was rescued by a single copy of Sup35Cp, was not rescued by Sup45p overexpression and was not associated with the appearance of Sup45-GFPp puncta. Paper-14004898.
We show that the C-terminal domain of the yeast cytoskeletal assembly protein Sla1 (Sla1C) specifically interacts with the N-terminal prion-forming domain (Sup35N) of the yeast release factor Sup35 (eRF3) in the two-hybrid system. Paper-8297314.
We show that the yeast Tsa1/ Tsa2 Prxs colocalize to ribosomes and function to protect the Sup35 translation termination factor against oxidative stress-induced formation of its heritable [ PSI(+)] prion conformation. Paper-14702448.
In agreement with the model postulating that excess Hsp104 acts on [ PSI ( + )] by disaggregating prion polymers, we show that an increase in Sup35 levels, accompanied by an increase in size of prion aggregates, also partially protects [ PSI(+)] from elimination by excess Hsp104. Paper-11366278.
We propose that Sup45p and Sup35p interact to form a release factor complex in yeast and that Sup35p, which has GTP binding sequence motifs in its C-terminal domain, provides the GTP hydrolytic activity which is a demonstrated requirement of the eukaryote translation termination reaction. Paper-360996.
Sla1(-) strains are sensitive to some translational inhibitors, and some sup35 mutants, obtained in a Sla1(-) background, are sensitive to Sla1, suggesting that the interaction between Sla1 and Sup35 proteins may play a role in the normal function of the translational apparatus. Paper-8297314.
Although overexpression of either the SUP45 or SUP35 genes alone did not reduce the efficiency of codon-specific tRNA nonsense suppression, the simultaneous overexpression of both the SUP35 and SUP45 genes in nonsense suppressor tRNA-containing strains produced an antisuppressor phenotype. Paper-360996.
These synonyms are used for gene SUP35 (Sup35p): SUP36, SUP2, SUF12, SAL3, PNM2, GST1.
These accession numbers are used for gene SUP35: .
SUP35 is a homologue of sup35 (translation release factor class II eRF3) from Schizosaccharomyces pombe 972h-.
SUP35 is a homologue of PF11_0245 (translation elongation factor EF-1, subunit alpha, putative) from Plasmodium falciparum 3D7.
SUP35 is a homologue of Os04g0270100 (Os04g0270100) from Oryza sativa Japonica Group.
SUP35 is a homologue of NCU04790 (eukaryotic peptide chain release factor GTP-binding subunit) from Neurospora crassa OR74A.
SUP35 is a homologue of MGG_00449 (hypothetical protein) from Magnaporthe oryzae 70-15.
SUP35 is a homologue of KLLA0D17424g (hypothetical protein) from Kluyveromyces lactis NRRL Y-1140.
SUP35 is a homologue of H19N07.1 (hypothetical protein) from Caenorhabditis elegans.
SUP35 is a homologue of gspt1l (G1 to S phase transition 1, like) from Danio rerio.
SUP35 is a homologue of GSPT1 (G1 to S phase transition 1) from Homo sapiens.
SUP35 is a homologue of GSPT1 (G1 to S phase transition 1) from Canis lupus familiaris.
SUP35 is a homologue of GSPT1 (G1 to S phase transition 1) from Bos taurus.
SUP35 is a homologue of GSPT1 (G1 to S phase transition 1) from Gallus gallus.
SUP35 is a homologue of Gspt1 (G1 to S phase transition 1) from Mus musculus.
SUP35 is a homologue of Gspt1 (G1 to S phase transition 1) from Rattus norvegicus.
SUP35 is a homologue of gspt1 (G1 to S phase transition 1) from Danio rerio.
SUP35 is a homologue of Elf (Ef1alpha-like factor) from Drosophila melanogaster.
SUP35 is a homologue of AT1G18070 (EF-1-alpha-related GTP-binding protein, putative) from Arabidopsis thaliana.
SUP35 is a homologue of AGOS_AGL145W (AGL145Wp) from Ashbya gossypii ATCC 10895.
SUP35 is a homologue of AgaP_AGAP009310 (AGAP009310-PA) from Anopheles gambiae str. PEST.
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