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At high concentrations, Hsp104 eliminates Sup35 prions. Paper-13049537.
Similarly to Sup35p, in [PSI+] cells Sup45p was found in aggregates. Paper-984099.
Interactions of the chaperone Hsp104 with yeast Sup35 and mammalian PrP. Paper-1267127.
Transcriptional regulation of SUP35 and SUP45 in Saccharomyces cerevisiae. Paper-1241871.
The [URE3] and [PSI(+)] prions are infectious amyloid forms of Ure2p and Sup35p. Paper-13257150.
These proteins ( Ure2p, Sup35p, and Rnq1p) share a set of remarkable properties. Paper-13148974.
Yeast [PSI+] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104. Paper-10098637.
[URE3] and [PSI] involve a self-propagating aggregation of Ure2p and Sup35p, respectively. Paper-2046421.
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.
Also in this respect SUP35 and SUP45 show a notable resemblance with ribosomal protein genes. Paper-1241871.
Ure2p and Sup35p are aggregated in vivo in [URE3]- and [PSI]-containing cells, respectively. Paper-8609076.
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.
Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers. Paper-10211370.
SUP35 and SUP45 encode translational release factors in the yeast Saccharomyces cerevisiae. Paper-1241871.
Suppression induced by extra- SUP35 and especially by extra- SUP45 is affected by the cell environment. Paper-69716.
For both Sup35 and Ure2, Hsp104 catalyzes de novo prion nucleation from soluble, native protein. Paper-12078866.
Propagation of the yeast prion [PSI+], a self-replicating aggregated form of Sup35p, requires Hsp104. Paper-11023955.
The yeast prions [URE3] and [PSI(+)] are self-propagating amyloids of Ure2p and Sup35p, respectively. Paper-12346114.
Guanidine reduces stop codon read-through caused by missense mutations in SUP35 or SUP45. Paper-9727850.
In contrast, Ssa1p together with either of its Hsp40 cochaperones blocks Sup35p polymerization. Paper-11376069.
In Saccharomyces cerevisiae, these proteins are encoded by the genes SUP45 and SUP35, respectively. Paper-13704170.
In both the Ure2p and Sup35p systems, prion domain amyloid filaments exhibit polymorphic variation. Paper-12366527.
Importance of low-oligomeric-weight species for prion propagation in the yeast prion system Sup35/ Hsp104. Paper-9948275.
A new omnipotent suppressor, SUP39, and alleles of sup35, sup45, SUP44 and SUP46 were identified. Paper-6379.
The possible mechanisms of interaction of the SUP1 and SUP2 genes with the [psi] determinant are discussed. Paper-39273.
Hsp104, Hsp70 and Hsp40 interplay regulates formation, growth and elimination of Sup35 prions. Paper-13049537.
Increased [PSI+] appearance by fusion of Rnq1 with the prion domain of Sup35 in Saccharomyces cerevisiae. Paper-13881558.
The SUP1 and SUP2 genes code for protein factors intimately involved in the control of translational accuracy. Paper-39273.
Both [URE3] and [PSI] appear to be due to self-propagating-amyloid formation of Ure2p and Sup35p, respectively. Paper-9202075.
3) Overproduction of Sup35p and Ure2p increases the frequency of cells acquiring [PSI] or [URE3], respectively. Paper-675509.
The interaction of Hsp104 with yeast prion fibers made of Sup35NM, a prion-inducing domain of Sup35, was tested. Paper-10872818.
Sup35 polymers contain Rnq1, confirming a hypothesis that Rnq1 polymers seed Sup35 polymerization. Paper-11281063.
Despite retention of [PSI(+)], excess Hsp104 decreases toxicity of overproduced Sup35 in [PSI(+)] strains. Paper-11366278.
These data are consistent with a model of [PSI+] induction caused by physical interactions between Rnq1p and Sup35p. Paper-13732991.
[URE3] and [PSI(+)] are infectious protein forms of the Saccharomyces cerevisiae Ure2p and Sup35p, respectively. Paper-10384545.
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.
The yeast [PSI(+)], [URE3], and [PIN(+)] genetic elements are prion forms of Sup35p, Ure2p, and Rnq1p, respectively. Paper-9207724.
Sup35 and Sup45 are essential protein components of the Saccharomyces cerevisiae translation termination factor. Paper-9727850.
In the yeast Saccharomyces cerevisiae, eRF1 and eRF3 are encoded by the SUP45 and SUP35 genes, respectively. Paper-9338609.
We show that Hsp104p greatly stimulates the assembly of Sup35p into fibrils, whereas Ydj1p has inhibitory effect. Paper-11376069.
It is widely believed that prion properties arise from the assembly of Ure2p, Sup35p and Rnq1p into insoluble fibrils. Paper-12821295.
Saccharomyces cerevisiae prion [PSI ] is a self-propagating isoform of the eukaryotic release factor eRF3 ( Sup35p). Paper-2166988.
For Ure2p and probably also Sup35p, the functional domain retains its globular fold but is inactivated by a steric mechanism. Paper-12366527.
The vital cellular role of Sup35p and Sup45p prompted us to study the regulation of transcription of the corresponding genes. Paper-1241871.
The CLN1, CLN2, and CLN3 genes of S. cerevisiae form a redundant family essential for the G1-to-S phase transition. Paper-33351.
In each case, the prion-associated phenotype has been linked to alternative conformations of the Ure2 and Sup35 proteins. Paper-8914462.
Chromosome stability in suppressor mutants for SUP35 and SUP45 genes coding for translation release factors was studied. Paper-8439427.
Here we report that Gpg1 blocks the maintenance of [PSI(+)], an aggregated prion form of the translation termination factor Sup35. Paper-13583186.
The products of the SUP45 ( eRF1) and SUP35 genes interact to mediate translation termination in Saccharomyces cerevisiae. Paper-360996.
Overexpression of the molecular chaperone Hsp104 abolishes the [PSI+] phenotype and restores the normal function of Sup35. Paper-11999313.
A protein-remodeling factor, Hsp104, controls the inheritance of several yeast prions, including those formed by Sup35 and Ure2. Paper-12078866.
The suppressors map at three loci, suf12, suf13, and suf14, which are located on chromosomes IV, XV, and XIV, respectively. Paper-3974558.
The inheritance of [PSI+] and the physical state of Sup35 in vivo depend on the protein chaperone Hsp104 ( heat shock protein 104). Paper-1267127.
The yeast prions [PSI+] and [PIN+] are self-propagating amyloid aggregates of the Gln/Asn-rich proteins Sup35p and Rnq1p, respectively. Paper-10558372.
Ure2p is partially protease-resistant in [URE3] strains and Sup35p is aggregated specifically in [PSI] strains supporting this idea. Paper-10570663.
Experiments with RNA isolated from yeast mutant with impaired splicing demonstrated that sup1 and sup2 genes do not contain introns. Paper-5164560.
The properties of Ure2p are compared in the discussion to that of other prion-like proteins such as Sup35 and mammalian prion protein PrP. Paper-1848149.
Absence of structural homology between sup1 and sup2 genes of yeast Saccharomyces cerevisiae and identification of their transcripts. Paper-5164560.
The [URE3] and [PSI+] prions of Saccharomyces cerevisiae are infectious amyloid forms of the proteins Ure2p and Sup35p, respectively. Paper-11023974.
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.
This activity is repressed in prion-infected cells for loss-of-activity prions, [URE3] (the prion of Ure2p) and [PSI] (the prion of Sup35p). Paper-12366527.
Overexpression of the SUP45 gene encoding a Sup35p-binding protein inhibits the induction of the de novo appearance of the [PSI+] prion. Paper-1363853.
The characterisation of both Sup35p and Ure2p, the two 'prion proteins', mainly focusing on their aggregation properties, support this model. Paper-8864322.
Interaction between yeast Sup45p ( eRF1) and Sup35p (eRF3) polypeptide chain release factors: implications for prion-dependent regulation. Paper-984099.
The introduction of such fibrils made from Ure2p or Sup35p into yeast cells leads to the prion phenotypes [URE3] and [PSI], respectively. Paper-13148974.
The SUP45 and SUP35 genes of Saccharomyces cerevisiae encode polypeptide chain release factors eRF1 and eRF3, respectively. Paper-984099.
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.
Nonsense mutations in the SUP35 gene do not lead to a decrease in levels of SUP35 mRNA and do not influence the steady-state level of eRF1. Paper-10869285.
The transcription activation sites of SUP35 and SUP45 were mapped using deletion analysis of the respective promoter-reporter fusion genes. Paper-1241871.
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.
CONCLUSIONS: These findings suggest the existence of an alternative, Hsp104-independent pathway to replicate non-Gln/Asn variant Sup35 prion seeds. Paper-9921044.
Depletion of a Drosophila homolog of yeast Sup35p disrupts spindle assembly, chromosome segregation, and cytokinesis during male meiosis. Paper-1495342.
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.
Overexpression of Hsp104 cures [PSI], as does the absence of this protein, suggesting that the prion change of Sup35p in [PSI] strains is aggregation. Paper-10570663.
Since the [PSI] state of the yeast strain affects the abundance of Sup35p and Sup45p, both [PSI+] and [psi-] variants were included in these analyses. Paper-1241871.
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.
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 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.
Indeed, like [PSI+], the maintenance of [ETA+] requires the N-terminal region of Sup35p and depends on an appropriate level of the chaperone protein Hsp104. Paper-1807441.
The overexpression of Hsp104p chaperone protein partially solubilizes Sup35P aggregates in the [psi+] strain, also causing an antisuppressor phenotype. Paper-601036.
Three different clones contained parts of the Q/N-rich amino-terminal domain of Mca1p/ Yca1p with the Sup35 part of the fusion protein partially inactive. Paper-13611737.
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.
Four fungal prion proteins have been studied in some depth- Ure2p, Sup35p, and Rnq1p of Saccharomyces cerevisiae and HET-s of Podospora anserina. Paper-12366527.
PNM2 is closely linked to the omnipotent suppressor gene SUP35 (also previously identified as SUP2, SUF12, SAL3 and GST1). Paper-132768.
At the molecular level, excess Ssa1 prevents a shift of Sup35 protein from the insoluble (prion) to the soluble (cellular) state in the presence of excess Hsp104. Paper-1718227.
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.
Over-expression of HAL3 in [ISP(+)] strain causes nonsense suppression, whereas its inactivation displays as anti-suppression of sup35 mutation in [isp(-)] strain. Paper-13162369.
Clearly, anti-suppression caused by growth in the presence of GuHCl is not sufficient to distinguish missense mutations in SUP35 or SUP45, from [PSI(+)]. Paper-9727850.
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.
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.
Dbp2p:Upf1p interaction occurs within a large conserved region in the middle of Upf1p that is largely distinct from its Nmd2p and Sup35/45p interaction domains. Paper-10707660.
It turned out that SUP35 and SUP45 transcript levels are regulated by nutritional changes and stress in a way strikingly similar to those of ribosomal protein genes. Paper-1241871.
Genetic evidence showed two non-Mendelian genetic elements of Saccharomyces cerevisiae, called [URE3] and [PSI], to be prions of Ure2p and Sup35p, respectively. Paper-2046421.
The structure of the C-domain of the X.laevis eRF3 protein is highly conserved with other Sup35-like proteins, as was also shown earlier for the eRF1 protein family. Paper-341815.
Perplexingly, deletion of Hsp104 eliminates Sup35 and Ure2 prions, whereas overexpression of Hsp104 purges cells of Sup35 prions, but not Ure2 prions. Paper-12078866.
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.
The previously described interaction between Sup35p and cytoskeletal assembly protein Sla1p points to the possible relationships between prions and cytoskeletal networks. Paper-8738362.
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.
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.
In Saccharomyces cerevisiae, translation termination is mediated by a complex of two proteins, eRF1 and eRF3, encoded by the SUP45 and SUP35 genes, respectively. Paper-859441.
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.
One model to explain this phenomenon proposes that, in the absence of Hsp104, Sup35p aggregates enlarge but fail to replicate thus becoming diluted out as the yeast divide. Paper-11023955.
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 proteins Ure2, Sup35 and Rnq1 from the baker's yeast have infectious properties, termed prions, at the origin of heritable and transmissible phenotypic changes. Paper-12821295.
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.
Here, we demonstrate that the yeast prion protein Sup35 interacts with various proteins of the actin cortical cytoskeleton that are involved in endocytosis. Paper-10841034.
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.
The N-terminal parts of Ure2p and Sup35p (the "prion domains") are responsible for prion formation and propagation and are rich in asparagine and glutamine residues. Paper-8609076.
Remarkably, Ure2 and Sup35 proteins existing in the alternative conformations have the unique capacity to transmit this physical state to the newly synthesized protein in vivo. Paper-8914462.
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.
Surprisingly, GuHCl and excess Hsp104, which are known to promote loss of [PSI(+)], did not prevent the de novo induction of [PSI(+)] by excess Sup35 in [psi(-)][PIN(+)] strains. Paper-8683737.
Six partially dominant antisuppressors were obtained that reduce the efficiency of two omnipotent yeast suppressors, sup45 and sup35, thought to be ribosomal ambiguity mutations. Paper-3442389.
Each prion data set was successfully fit with the F-W model, including three different yeast prion proteins ( Sup35p, Ure2p, and Rnq1p) as well as mouse and human prions. Paper-13015678.
Such GuHCl-remedial Mendelian suppressors were selected under conditions where [PSI(+)] appearance was limiting, and were caused by missense mutations in SUP35 or SUP45. Paper-9727850.
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.
The aggregation of the two yeast proteins Sup35p and Ure2p is widely accepted as a model for explaining the prion propagation of the phenotypes [PSI+] and [URE3], respectively. Paper-9154472.
Such Q/N-rich domains are found in two other yeast prion proteins, Sup35p and Rnq1p, although none of the many other yeast Q/N-rich domain proteins have yet been found to be prions. Paper-10494326.
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.
From these and our previous data, we propose that yeast Sup45 and Sup35 proteins belonging to eRF1 and eRF3 protein families respectively are also yeast termination factors. Paper-341815.
However, GFP fusions with highly aggregatable, prion-determining, and highly charged sequences from yeast prions, such as Sup35 and Ure2p, form green fibrils with properly folded GFP. Paper-12774334.
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.
Latrunculin A influences neither the levels of total cellular Sup35p nor the levels of chaperone proteins, such as Hsp104 and Hsp70, which were previously shown to affect [PSI]. Paper-8738362.
[URE3] is an altered infectious form of the Ure2 protein, a regulator of nitrogen catabolism, while [PSI] is a prion of the Sup35 protein, a subunit of the translation termination factor. Paper-8609076.
Like the prion domains of Sup35p and Ure2p, Rnq1p is rich in N and Q residues, but rnq1Delta strains have no known phenotype except for inability to propagate the [PIN(+)] prion. Paper-12751501.
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.
Yeast infectious protein (prion) forms of the Ure2 and Sup35 proteins determine the nonchromosomal genes [URE3] and [PSI], and these are, therefore, the basis for a kind of epigenetic phenomena. Paper-9202075.
This approach is illustrated with [URE3], an amyloid-based prion of the regulator of nitrogen catabolism, Ure2p and [PSI(+)] as a prion of the translation termination factor Sup35p. Paper-12061274.
Mutational alterations of the cortical actin cytoskeleton decrease aggregation of overproduced Sup35 and de novo prion induction and increase prion-related toxicity in yeast. Paper-10841034.
The yeast non-Mendelian factor [ETA+] is lethal in the presence of certain mutations in the SUP35 and SUP45 genes, which code for the translational release factors eRF3 and eRF1, respectively. Paper-1807441.
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.
In vivo propagation of [PSI(+)], an aggregation-prone prion isoform of the yeast release factor Sup35 (eRF3), has previously been shown to require intermediate levels of the chaperone protein Hsp104. Paper-8994441.
In parallel with these homology effects, which act at the level of DNA or RNA, elevated copy number of the Ure2 and Sup35 proteins increases the frequency of their own "silencing" by prion formation. Paper-9202075.
We show that these genes are the equivalents of the SUP35 and SUP45 genes of Saccharomyces cerevisiae, which encode the cytosolic translation termination factors eRF3 and eRF1, respectively. Paper-1558751.
When the prion-like region of Rnq1 was substituted for the prion domain of Sup35, the protein determinant of the prion [PSI+], the phenotypic and epigenetic behavior of [PSI+] was fully recapitulated. Paper-2122102.
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.
Their genetic properties led us to propose that they are prions, altered self-propagating forms of Ure2p and Sup35p, respectively, that cannot properly carry out the normal functions of these proteins. Paper-10570663.
Propagation of the yeast protein-based non-Mendelian element [PSI], a prion-like form of the release factor Sup35, was shown to be regulated by the interplay between chaperone proteins Hsp104 and Hsp70. Paper-2050486.
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.
Oligopeptide repeats within the Sup35 N-terminal domain (PrD) presumably are required for the stable [PSI+] inheritance that in turn involves fragmentation of Sup35 polymers by the chaperone Hsp104. Paper-11379563.
2) [PSI] propagation requires SUP35 and [URE3] propagation requires URE2 with recessive chromosomal mutants having the same phenotypes as the presence of the respective dominant non-Mendelian element. Paper-675509.
Unlike [PSI(+)] variants, where the strength of translation termination corresponds to the level of soluble Sup35, the phenotypes of these [PIN(+)] variants do not correspond to levels of soluble Rnq1. Paper-9271826.
Complementation of the mutant with a double disruption of SUP35 and SUP45 genes is obtained when mGSPT2 and human eRF1 are co-expressed but not by co-expression of mGSPT1 and human eRF1. Paper-9322952.
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.
However, ubc4Delta increases the proportion of the Hsp70 chaperone Ssa bound to Sup35, suggesting that misfolded Sup35 is either more abundant or more accessible to the chaperones in the absence of Ubc4. Paper-12441689.
We show here that Ure2p is a soluble protein that can assemble into fibers that are similar to the fibers observed in the case of PrP in its scrapie prion filaments form or that form on Sup35 self-assembly. Paper-1848149.
The Sup35N-Sla1C interaction is inhibited by Sup35N alterations that make Sup35 unable to propagate the [PSI(+)] state and by the absence of the chaperone protein Hsp104, which is essential for [PSI] propagation. 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.
Analysis of the naturally occurring alleles of RNQ1 and SUP35 indicated that the various polymorphisms identified were associated with DNA tandem repeats (6, 12, 33, 42 or 57 bp) within the coding sequences. Paper-9948065.
Saccharomyces cerevisiae can be infected with four amyloid-based prions: [URE3], [PSI(+)], [PIN(+)], and [SWI(+)], due to self-propagating aggregation of Ure2p, Sup35p, Rnq1p and Swi1p, respectively. Paper-13611737.
Filament polymorphism appears to underlie the phenomenon of prion "variants" which differ in the severity of their phenotype, that is, for Ure2p and Sup35p, the stringency with which their activity is switched off. Paper-12366527.
The maintenance of [PSI], a prion-like form of the yeast release factor Sup35, requires a specific concentration of the chaperone protein Hsp104: either deletion or overexpression of Hsp104 will cure cells of [PSI]. Paper-1718227.
Both C1054U and two previously described yeast 18S rRNA antisuppressor mutations, G517A (rdn-2) and U912C (rdn-4), inhibited codon-nonspecific suppression caused by mutations in eukaryotic release factors, sup45 and sup35. Paper-551719.
However, diploids and meiotic progeny from crosses between either different [PSI(+)], or different [PIN(+)] variants, always have the phenotype of the parental variant with the least soluble Sup35 or Rnq1, respectively. Paper-9271826.
The S. cerevisiae prion states [PSI(+)] and [URE3] arise from aggregation of the proteins Sup35p and Ure2p respectively, and correlate with the ability of Sup35p and Ure2p to form amyloid-like fibrils in vitro. Paper-13487218.
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 propose that Hsp104p plays a role in establishing stable [psi+] inheritance by splitting up Sup35p aggregates and thus ensuring equidistribution of the prion-like Sup35p isoform to daughter cells at cell divisions. Paper-601036.
We also show that the "prion-inducing domain" of Sup35p is in the N-terminal region, which, like the "prion-inducing domain" of another yeast prion, Ure2p, was previously shown to be distinct from the functional domain of the protein. Paper-927037.
This is half the packing density of approximately 1 subunit per 0.47 nm previously obtained for fibrils of the yeast prion proteins, Ure2p and Sup35p, whence it follows that the respective amyloid architectures are basically different. Paper-13114682.
Our observations reveal the functional differences between Hsp104p and the Hsp70-40 systems in the assembly of Sup35p into fibrils and bring new insight into the mechanism by which molecular chaperones influence the propagation of [PSI+]. Paper-11376069.
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.
Taken together, our data suggest that phosphorylation of Mcm2 and probably other members of the Mcm2-7 proteins by Cdc7- Dbf4 at the G1-to-S phase transition is a critical step in the initiation of DNA synthesis at replication origins. Paper-1288581.
A large amount of data have been produced, from which it was concluded that the SUP45 and SUP35 genes were controlling translation termination but were also involved in other functions important for the cell organization and the cell cycle accomplishment. Paper-9932046.
In the budding yeast Saccharomyces cerevisiae, various proteins have prion properties and adopt atypical phenotypes as genetic elements, such as the Sup35 and Ure2 proteins, corresponding to the [PSI(+)] and [URE3] phenotypes, respectively. Paper-13659560.
Indeed, we show that newly forming Sup35 and preexisting Rnq1 aggregates always colocalize when [PSI+] appearance is facilitated by the [RNQ+] prion, and that Rnq1 fibers enhance the in vitro formation of fibers by the prion domain of Sup35 (NM). Paper-10652273.
We further demonstrate that the negative effect of heat stress on [PSI(+)] phenotype directly correlates with solubility of Sup35p and find that in wild-type strains the presence of [PSI(+)] causes a stress that elevates basal expression of Hsp104 and SSA1. Paper-8594264.
We show that recombinant Ure2p is a soluble protein that can assemble in vitro into dimers, tetramers, and octamers or form insoluble fibrils observed for PrP in its filamentous form or for Sup35p upon self-assembling, suggesting a similar mechanism for all prions. Paper-2115987.
Translation termination factors eRF1 (Sup45) and eRF3 ( Sup35) participate not only in the last step of protein synthesis but also in mRNA degradation and translation initiation via interaction with such proteins as Pab1, Upf1, Upf2 and Upf3. Paper-12528872.
The five suppressors SUP35, SUP43, SUP44, SUP45 and SUP46, each mapping at a different chromosomal locus in the yeast Saccharomyces cerevisiae, suppress a wide range of mutations, including representatives of all three types of nonsense mutations, UAA, UAG and UGA. Paper-5183400.
The loss of Sup35([PSI+]) remodeling by Hsp104 decreases the mobility of these complexes in the cytosol, creates a segregation bias that limits their transmission to daughter cells, and consequently diminishes the efficiency of conversion of newly made Sup35 to the prion form. Paper-13110693.
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.
Respiratory deficiency of MB43-nam9-1 is overcome by transient overexpression of HSP104, by deletion of HSP104, by transient exposure to guanidine hydrochloride, and by expression of the C-terminal portion of Sup35, indicating an involvement of the yeast prion [PSI(+)]. Paper-8384554.
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.
Recent work suggests that two unrelated phenotypes, [PSI+] and [URE3], in the yeast Saccharomyces cerevisiae are transmitted by non-covalent changes in the physical states of their protein determinants, Sup35p and Ure2p, rather than by changes in the genes that encode these proteins. Paper-2124648.
We have demonstrated that ribosomes from the four suppressors SUP35, SUP44, SUP45 and SUP46 translate polyuridylate templates in vitro with higher errors than ribosomes from the normal stain, and that this misreading is substantially enhanced by the antibiotic paromomycin. Paper-5183400.
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.
We have recently shown that Hsp104 interacts preferably with low oligomeric species of a Sup35 derived peptide, Sup35[5-26]; however, due to possible exchange between different oligomeric states, it was not possible to obtain information on the distribution and stability of the oligomeric state. Paper-11999313.
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.
Based on these and other data, we propose a two-cycle model for "prionization" of Sup35p in [PSI(+)] cells: cycle A is the GdnHCl-sensitive ( Hsp104-dependent) replication of the prion seeds, while cycle B is a GdnHCl-insensitive ( Hsp104-independent) process that converts these seeds to pelletable aggregates. Paper-9215204.
Here we show that deletion of the UBP6 gene in Saccharomyces cerevisiae causes sensitivity to a broad range of toxic compounds and antagonizes phenotypic expression and de novo induction of the yeast prion [PSI+], a functionally defective self-perpetuating isoform of the translation termination factor Sup35. Paper-10042288.
In contrast to the ribosomes from the four suppressors SUP35, SUP44, SUP45 and SUP46, the ribosomes from the SUP43 suppressor do not significantly misread polyuridylate templates in vitro, suggesting that this locus may not encode a ribosomal component or that the misreading is highly specific. Paper-5183400.
One and the same chaperone alteration, substitution A503V in the middle region of the chaperone Hsp104, exhibited opposite effects on one of the endogenous prions ([PSI(+)], the prion form of Sup35) and on polyglutamines, increasing aggregate size and toxicity in the former case and decreasing them in the latter case. Paper-10796535.
Saccharomyces cerevisiae is host to the dsRNA viruses L-A (including its killer toxin-encoding satellite, M) and L-BC, the 20S and 23S ssRNA replicons, and the putative prions, [URE3] and [PSI]. review the genetic and biochemical evidence indicating that [URE3] and [PSI] are prion forms of Ure2p and Sup35p, respectively. Paper-907150.
Effective expression of the HIV-1 core protein Gag-p55 was obtained in Saccharomyces cerevisiae under control of the inducible UASgal/ CYC1 promoter as a translational fusion with the prion-forming NM domain of the translation terminator Sup35p (eRF3) of S. cerevisiae. where only poor expression of the original-type Gag-p55 was observed. Paper-8812933.
In vitro, Ure2p and Sup35p form amyloid, a filamentous protein structure, high in beta-sheet with a characteristic green birefringent staining by the dye Congo Red. Amyloid deposits are a cardinal feature of Alzheimer's disease, non-insulin-dependent diabetes mellitus, the transmissible spongiform encephalopathies, and many other diseases. Paper-2046421.
These synonyms are used for gene SUP35 (Sup35p): YDR172W, YD9395.05, Translation release factor 3, SUP36, SUP2, SUF12, SAL3, Polypeptide release factor 3, PNM2, Omnipotent suppressor protein 2, GST1, G1 to S phase transition protein 1, Eukaryotic peptide chain release factor GTP-binding subunit, ERF-3, ERF3, ERF2.
These accession numbers are used for gene SUP35: P05420 (UNIPROT__AC), CAA86677 (NCBI_GENBANK__AC), CAA30155 (NCBI_GENBANK__AC).
SUP35 is a homologue of PF11_0245 (translation elongation factor EF-1, subunit alpha) 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 grisea 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 Bos taurus.
SUP35 is a homologue of GSPT1 (G1 to S phase transition 1) from Pan troglodytes.
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 Canis lupus familiaris.
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 erf3 (translation release factor eRF3 (class II) (PMID 9701287)) from Schizosaccharomyces pombe.
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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iHOP - Information Hyperlinked over Proteins .
Concept & Implementation by Robert Hoffmann.