The Sup35 (eRF3) translation termination factor of Saccharomyces cerevisiae can undergo a prion-like conformational conversion, thus resulting in the [PSI +] nonsense-suppressor determinant.In vivo this process depends critically on the chaperone Hsp104, whose lack or overexpression can cure [PSI +]. The use of artificial prion [PSI +PS] based on a hybrid Sup35PS with prion domain from the yeast Pichia methanolicaallowed us to uncover three more chaperones, Ssb1, Ssa1, and Ydj1, whose overexpression can cure prion determinants. Here, we used the [PSI +PS] to search a multicopy yeast genomic library for novel factors able to cure prions. It was found that overexpression of the Hsp40 family chaperones Sis1 and Ynl077w, chaperone Sti1, transcriptional factors Sfl1 and Ssn8, and acidic ribosomal protein Rpp0 can interfere with propagation and manifestation of [PSI +PS] in a prion strain-specific manner. Some of these factors also affected the manifestation and propagation of conventional [PSI +]. Excess of Sfl1, Ssn8, and Rpp0 influenced at least one of the tested chaperone-specific promoters,SSA4, HSP104, and model promoters, with either the heat shock or stress response elements. Thus, the induction of chaperone expression by these proteins could explain their prion-curing effects. The Sup35 (eRF3) translation termination factor of Saccharomyces cerevisiae can undergo a prion-like conformational conversion, thus resulting in the [PSI +] nonsense-suppressor determinant.In vivo this process depends critically on the chaperone Hsp104, whose lack or overexpression can cure [PSI +]. The use of artificial prion [PSI +PS] based on a hybrid Sup35PS with prion domain from the yeast Pichia methanolicaallowed us to uncover three more chaperones, Ssb1, Ssa1, and Ydj1, whose overexpression can cure prion determinants. Here, we used the [PSI +PS] to search a multicopy yeast genomic library for novel factors able to cure prions. It was found that overexpression of the Hsp40 family chaperones Sis1 and Ynl077w, chaperone Sti1, transcriptional factors Sfl1 and Ssn8, and acidic ribosomal protein Rpp0 can interfere with propagation and manifestation of [PSI +PS] in a prion strain-specific manner. Some of these factors also affected the manifestation and propagation of conventional [PSI +]. Excess of Sfl1, Ssn8, and Rpp0 influenced at least one of the tested chaperone-specific promoters,SSA4, HSP104, and model promoters, with either the heat shock or stress response elements. Thus, the induction of chaperone expression by these proteins could explain their prion-curing effects. heat shock element stress response element There are several proteins in the yeast Saccharomyces cerevisiae, which, similar to mammalian prions, can undergo autocatalytic conformational rearrangement. This process can last stably for many cellular generations, resulting in some cases in heritable phenotypes (1Wickner R.B. Taylor K.L. Edskes H.K. Maddelein M.L. Moriyama H. Roberts B.T. J. Struct. Biol. 2000; 130: 310-322Crossref PubMed Scopus (67) Google Scholar). The most studied of the yeast prion proteins is the translation termination factor Sup35 (eRF3), which is related to the [PSI +] determinant. The prion state of Sup35 is characterized by its aggregation and partial inactivation, which causes the nonsense-suppressor [PSI +] phenotype (2Patino M.M. Liu J.J. Glover J.R. Lindquist S. Science. 1996; 273: 622-626Crossref PubMed Scopus (572) Google Scholar, 3Paushkin S.V. Kushnirov V.V. Smirnov V.N. Ter-Avanesyan M.D. EMBO J. 1996; 15: 3127-3134Crossref PubMed Scopus (469) Google Scholar). Different [PSI +] isolates (“strains”) may vary in the efficiency of suppression, which presumably reflects different structures of Sup35 aggregates. The [PSI +] strains with strong suppression (“strong”) are highly stable, the strains with weak suppression (“weak”) show decreased mitotic stability (4Derkatch I.L. Chernoff Y.O. Kushnirov V.V. Inge-Vechtomov S.G. Liebman S.W. Genetics. 1996; 144: 1375-1386Crossref PubMed Google Scholar, 5Kochneva-Pervukhova N.V. Chechenova M.B. Valouev I.A. Kushnirov V.V. Smirnov V.N. Ter-Avanesyan M.D. Yeast. 2001; 18: 489-497Crossref PubMed Scopus (58) Google Scholar). Studies of the yeast prions confirmed that they reproduce the basic properties of their mammalian prototype and also show profound similarities to another related phenomenon, amyloids. In particular, purified Sup35 formed amyloid fibers in vitro (6Glover J.R. Kowal A.S. Schirmer E.C. Patino M.M. Liu J.J. Lindquist S. Cell. 1997; 89: 811-819Abstract Full Text Full Text PDF PubMed Scopus (543) Google Scholar). Therefore, Sup35 could be used as a convenient model for studying the basic features of both the prion and amyloid phenomena, and it is likely that the cellular factors interfering with the propagation of yeast prions are similar to those that can interfere with the prion or amyloid formation in animals. Although in vitro Sup35 alone is sufficient for its conformational rearrangement, in vivo some cellular proteins can participate in this process and modulate its efficiency. The most important of them is the Hsp104 chaperone, which is strictly required for the [PSI +] propagation, although its excess interferes with [PSI +] (7Chernoff Y.O. Lindquist S.L. Ono B. Inge-Vechtomov S.G. Liebman S.W. Science. 1995; 268: 880-884Crossref PubMed Scopus (925) Google Scholar). The chaperones of the Hsp70 family showed weaker effects; the overexpression of Ssb1 cured weak [PSI +] strains (8Chacinska A. Szczesniak B. Kochneva-Pervukhova N.V. Kushnirov V.V. Ter-Avanesyan M.D. Boguta M. Curr. Genet. 2001; 39: 62-67Crossref PubMed Scopus (45) Google Scholar, 9Kushnirov V.V. Kryndushkin D.S. Boguta M. Smirnov V.N. Ter- Avanesyan M.D. Curr. Biol. 2000; 10: 1443-1446Abstract Full Text Full Text PDF PubMed Scopus (129) Google Scholar), whereas overproduction of Ssa1 interfered with the [PSI +] curing by excess Hsp104 (10Newnam G.P. Wegrzyn R.D. Lindquist S.L. Chernoff Y.O. Mol. Cell. Biol. 1999; 19: 1325-1333Crossref PubMed Scopus (229) Google Scholar). Mutational alterations of Hsp104 and Ssa1 could also cause [PSI +] elimination (7Chernoff Y.O. Lindquist S.L. Ono B. Inge-Vechtomov S.G. Liebman S.W. Science. 1995; 268: 880-884Crossref PubMed Scopus (925) Google Scholar, 11Jung G. Jones G. Wegrzyn R.D. Masison D.C. Genetics. 2000; 156: 559-570PubMed Google Scholar). Construction of heterologous [PSI +] ([PSI +PS]) provided a sensitive instrument for identification of novel factors involved in the prion propagation. [PSI +PS] is based on a hybrid Sup35, in which the native prion domain was replaced with its analog from the yeast Pichia methanolica (12Kushnirov V.V. Kochneva-Pervukhova N.V. Chechenova M.B. Frolova N.S. Ter-Avanesyan M.D. EMBO J. 2000; 19: 324-331Crossref PubMed Scopus (136) Google Scholar). Compared with [PSI +], [PSI +PS] showed increased sensitivity to overexpression of the Hsp70 chaperones Ssa1 and Ssb1 and the Hsp40 chaperone Ydj1 but decreased sensitivity to the excess Hsp104 (9Kushnirov V.V. Kryndushkin D.S. Boguta M. Smirnov V.N. Ter- Avanesyan M.D. Curr. Biol. 2000; 10: 1443-1446Abstract Full Text Full Text PDF PubMed Scopus (129) Google Scholar). The [PSI +PS] curing by chaperones showed remarkable prion strain specificity. The chaperones ranked differently by their curing efficiency for each prion strain. This finding supports the existence of different prion structures corresponding to prion strains and differential sensitivity of these structures to curing mechanisms associated with different chaperones. Thus, the sets of chaperones able to cure a given prion may differ for different prions and prion strains. [URE3] prion was cured by overproduced Ydj1 but was insensitive to excess Hsp104 (13Moriyama H. Edskes H.K. Wickner R.B. Mol. Cell. Biol. 2000; 20: 8916-8922Crossref PubMed Scopus (240) Google Scholar). Recent studies of [RNQ+ ] showed that it depends on another chaperone of the Hsp40 family, Sis1, which has not been found among the factors curing [PSI +] (14Sondheimer N. Lopez N. Craig E.A. Lindquist S. EMBO J. 2001; 20: 2435-2442Crossref PubMed Scopus (169) Google Scholar). Deletion of the inessential glycine- and phenylalanine-rich region of Sis1 abolished propagation of this prion. It should be noted that all mentioned chaperones are considered to be related functionally. Hsp70 and Hsp40 represent eukaryotic homologues of the bacterial chaperone system DnaK-DnaJ, and Ydj1 and Sis1 are presumed to be partners for Ssa1 (15Lu Z. Cyr D.M. J. Biol. Chem. 1998; 273: 27824-27830Abstract Full Text Full Text PDF PubMed Scopus (187) Google Scholar). In vitro, Ssa1 and Ydj1 cooperated with Hsp104 to reactivate the aggregates of heat-denatured luciferase, with each of the chaperones being essential for this process (16Glover J.R. Lindquist S. Cell. 1998; 94: 73-82Abstract Full Text Full Text PDF PubMed Scopus (1103) Google Scholar). To find additional factors that can influence the prion propagation in yeast and presumably in other organisms we decided to use the potential of the [PSI +PS] system to perform a systematic screen for the genes that cure [PSI +PS] when overexpressed. The search revealed genes coding for two chaperones of the Hsp40 family, Sis1 and previously uncharacterized Ynl077w, Sti1 chaperone, transcriptional factors Sfl1 and Ssn8, and acidic ribosomal protein Rpp0. The following yeast strains were used: 5V-H19 (MATa ade2–1 SUQ5 ura3–52 leu2–3,112 can1–100 [psi −]), PS-5V-H19 (obtained from 5V-H19 by replacing SUP35 for the chimericalSUP35-PS allele), and their derivatives carrying independently isolated [PSI +] variants, weak and strong determinants ([PSI +W] and [PSI +S]) in 5V-H19 and strong [PSI +PS-1] and [PSI +PS-2] variants in PS-5V-H19 (12Kushnirov V.V. Kochneva-Pervukhova N.V. Chechenova M.B. Frolova N.S. Ter-Avanesyan M.D. EMBO J. 2000; 19: 324-331Crossref PubMed Scopus (136) Google Scholar). Strain 1A-H74 (MATα ade2–1 SUQ5 ura3–52 leu2–3,112 his3 SUP35-PS[PSI +PS-1]) was derived from a cross between strains PS-5V-H19 [PSI +PS-1] and 4V-H73 [psi (12Kushnirov V.V. Kochneva-Pervukhova N.V. Chechenova M.B. Frolova N.S. Ter-Avanesyan M.D. EMBO J. 2000; 19: 324-331Crossref PubMed Scopus (136) Google Scholar). were at in or were used in Genetics. Scholar). of yeast was as R.D. Yeast. 1995; PubMed Scopus Google Scholar). To the [PSI +] with each were on in Genetics. to the and on The of [PSI +] or [PSI +PS] was as a of and least of each were or more for cases of To the were on for and the and the were for more of and yeast by of and were as J. Scholar). genomic based on the multicopy and were used V.N. Valouev I.A. S.V. Kushnirov V.V. Smirnov V.N. Ter-Avanesyan M.D. Mol. Biol. 2001; PubMed Scopus Google Scholar, J. Genetics. 1998; Google Scholar). the library isolated in the the following genomic for the prion-curing were the R.D. A. PubMed Scopus Google for the and the was in two was by with and and the of A. D.M. PubMed Scopus Google of the the of this was of R.D. A. PubMed Scopus Google Scholar). was by the of M.D. Kushnirov V.V. Chernoff Y.O. Inge-Vechtomov S.G. Smirnov V.N. Mol. PubMed Scopus Google the and of genomic this was with The the the of Mol. 2001; PubMed Scopus Google was a of The of the was the and to the The and based on M. Mol. Cell. Biol. PubMed Scopus Google were a of H. The of each the and a were with the of the resulting in the and used The was as The of was the corresponding of the the of Yeast. PubMed Scopus Google Scholar), the was the coding region of the by with The from this was used to the genomic was by J. Scholar). a from was with genomic with and the a of was the in of the of from this was used to the genomic The was confirmed by of of from with genomic with were in or in a for to of The were in and by in was by at for To the protein in the was to M.M. PubMed Scopus Google Scholar, To the of were with for and by in with and The were by a of ribosomal in the was with The of Rpp0 was revealed by a Rpp0 of G. proteins were on to PubMed Scopus Google and to was the was as A. J. PubMed Scopus Google that the were by them to two and a at Sfl1 the was the and of to strain with this was to of at and Sfl1 expression was by of to at were by for at in of with and to two was to a of and was to a of The was on for and at for at to The protein was purified from the of to the from the The of the protein was confirmed by with were as PubMed Scopus Google Scholar). To and and were by the region and the region was in with in the of The protein or yeast were with of the or for at in of were by in a at in for The was on and to at The strain 5V-H19 and its were used in this strains the ade2–1 and the but differ from each other by the SUP35 The strain the of the conventional [PSI +], whereas its the hybrid of this for propagation of [PSI +PS] (12Kushnirov V.V. Kochneva-Pervukhova N.V. Chechenova M.B. Frolova N.S. Ter-Avanesyan M.D. EMBO J. 2000; 19: 324-331Crossref PubMed Scopus (136) Google ade2–1 in with [PSI +] or [PSI which in and The these determinants and The strain PS-5V-H19 [PSI +PS-1] was with two S. cerevisiae genomic based on the multicopy and of were of factors interfering with the [PSI +PS] should either cure [PSI +PS] or the prion conversion, increased of with should or in to of other were and by To the and [PSI +PS] curing from [PSI +PS] two of each were to a 1A-H74 [PSI +PS-1] strain. In this the that [PSI +PS-1] should [PSI +PS] were or in and were used for The were used to the PS-5V-H19 [PSI +PS-1] and of them or were from the of genomic and the were by of the with the yeast at the several the genes [PSI +PS] were by The following genes were two one one one one one three Sup35, causes but not [PSI +PS] Sup35 not in [PSI +PS] and not interfere with Sup35PS prion aggregation (12Kushnirov V.V. Kochneva-Pervukhova N.V. Chechenova M.B. Frolova N.S. Ter-Avanesyan M.D. EMBO J. 2000; 19: 324-331Crossref PubMed Scopus (136) Google Scholar). a previously uncharacterized protein of the Hsp40 family as The other genes Hsp40 chaperone Sis1, chaperone Sti1, transcriptional factors Sfl1 and Ssn8, and acidic ribosomal protein Rpp0. The of overproduction of these and prion were characterized for the independently isolated strains of hybrid and conventional [PSI +] not [PSI excess Sis1 showed whereas excess Rpp0 the prion but It should be noted as it was previously (9Kushnirov V.V. Kryndushkin D.S. Boguta M. Smirnov V.N. Ter- Avanesyan M.D. Curr. Biol. 2000; 10: 1443-1446Abstract Full Text Full Text PDF PubMed Scopus (129) Google Scholar), the efficiency of chaperones in prion curing on the [PSI +] strain and the of Sup35 prion The of excess Sis1 was by in the of Sup35PS which that Sis1 interfered with the prion of the +] were for the of [PSI +] strains The of was by the of yeast on for and the can The of prion was as not of the for prion reflects a of in strong weak with the in a The were for the of [PSI +] strains The of was by the of yeast on for and the can The of prion was as not of the for prion reflects a of in strong weak with the Although all previously prion-curing factors represent chaperones, the Sfl1 and proteins to a different being involved in transcriptional Sfl1 is a of a transcriptional factor the heat shock a that to the transcriptional S. R.D. S. A. 1995; PubMed Scopus Google Scholar). and Sfl1 and in of the expression M. EMBO J. 1998; PubMed Scopus Google Scholar). To the of Sfl1 and Ssn8, the and genes were by of the in the strain PS-5V-H19 [PSI The with showed This was [PSI the to on or with the Sup35 the prion The could be of prion In this we decreased of Sup35PS in the PS-5V-H19 [PSI strain with [PSI we could not this the Sup35PS in these strains were and to the other the affected in the PS-5V-H19 [psi it showed increased of with [psi not not the suppression of ade2–1 and not of the [psi but it is likely in with [PSI which is a strong it could be In the of were by increased and phenotypes were for the S. A. 1998; PubMed Scopus Google Scholar), and the was in M. Genetics. PubMed Google Scholar), whereas the of the is a novel response to heat shock is by of to the of S. G. Scholar). The of Sfl1 to that Sfl1 could also to and the expression of heat a was studied by was as of Sfl1 was as was with Sfl1 or yeast in the of Sfl1 and on a showed to Sfl1, which that Sfl1 can the also some of yeast and the of with the Sfl1 This that Sfl1 was a of these with some other the of the was that of the The of the in the Sfl1 was to the This that the Sfl1 was a protein to In Sfl1 not to another element of many and S. G. Scholar). the of protein to in the on the Sfl1 being the in the This that although Sfl1 not it a influence on the Rpp0 one of the acidic ribosomal proteins that a at the of a yeast Rpp0 a it is essential for and of other acidic ribosomal proteins to the it was that the increased not to increased of Rpp0 and its from J. Biol. Chem. Full Text PDF PubMed Google Scholar). a a of of multicopy Therefore, we studied the of Rpp0 and its The of Rpp0 revealed excess of it in the of with multicopy The were by a and the ribosomal were by the of ribosomal This finding Rpp0 in not in a The of Rpp0 was in a and in the one Rpp0. Therefore, the multicopy expression of to the of Rpp0 in the of This not strictly the J. Biol. Chem. Full Text PDF PubMed Google of the use of different expression J. Biol. Chem. Full Text PDF PubMed Google used a which presumably should a Rpp0 expression In the prion curing was of the of proteins involved in the prion propagation. The studied factors either to proteins or by expression of the proteins of this The likely for the chaperones Sis1, and Sti1, whose is to the protein The for the transcriptional factors Sfl1 and Ssn8, as as for the ribosomal protein Rpp0. Although Rpp0 is not a transcriptional its influence on expression may be the lack of acidic ribosomal proteins and and related to the of many chaperones. a of the the [PSI +PS] could be of decreased expression of we the [PSI +] at decreased Sup35 we found that the overexpression of Ssn8, Sfl1, and Rpp0 not the Sup35 not the overexpression of Rpp0 increased Sup35 which should the prion of the and of the chaperone of of the of was in the PS-5V-H19 [psi with alterations of the The most with the are given in with the in a of the of was in the PS-5V-H19 [psi with alterations of the The most with the are given in with the Sfl1 and expression of the chaperone they the of many chaperones, and the curing of prions likely be of a of in the of several chaperones, of It is that expression of the genes is by either one or of the two and S. G. Scholar). To the of overproduced Sfl1, Ssn8, and Rpp0 on the chaperone we their influence on the of expression the of model either or also tested the and is of a heat shock or stress and is for its and essential in prion propagation. Excess Sfl1 increased the expression which is with its to the and that Sfl1 as transcriptional Excess Sfl1 also increased the Excess not the of expression but the and the The lack of Ssn8, the and with its Excess Rpp0 increased the and expression to the as excess of Sfl1, Ssn8, and Rpp0 affected the expression of chaperones, they are also likely to the to heat To we tested the of with increased or decreased of Sfl1, Ssn8, and Rpp0 to at this of of yeast may in the of the S. A. 2001; PubMed Scopus Google Scholar). Although the PS-5V-H19 [psi not at the of multicopy with but not them to at this was for derivatives of this strain or In this a search for the cellular factors interfering with the [PSI +PS] propagation was Although previously chaperones Ssb1, Ssa1, and were as this search in to chaperones Sis1, and Sti1, transcriptional factors Sfl1 and Ssn8, and acidic ribosomal protein Rpp0. that all revealed factors could either by interfering with the Sup35PS prion or by the of the proteins involved in this The likely for the chaperones, whereas the likely for the transcriptional factors and the ribosomal of the three found chaperones, Sis1 and to the Hsp40 family to bacterial this is a of a and it supports a chaperone of this to Ydj1 among yeast of were in this the [PSI +PS] curing and the was for the The the efficiency of prion we found increased of Sup35 in the corresponding [PSI +PS] It is likely that the three considered Hsp40 proteins in prion they could with Hsp104 and Hsp70 in of prion aggregates (14Sondheimer N. Lopez N. Craig E.A. Lindquist S. EMBO J. 2001; 20: 2435-2442Crossref PubMed Scopus (169) Google Scholar). It is of to that whereas the of Sis1 was that of Ydj1, Sis1 is at Ydj1, which a Hsp40 in yeast Craig E.A. Mol. Cell. Biol. 1999; 19: PubMed Scopus Google Scholar). Thus, Sis1 are more in prion chaperones of the Hsp70 family were found in this This is not these chaperones are and a of their expression Hsp40 chaperones. Ssa1 a weak and Ssb1 on [PSI +PS-1] used in the screen (9Kushnirov V.V. Kryndushkin D.S. Boguta M. Smirnov V.N. Ter- Avanesyan M.D. Curr. Biol. 2000; 10: 1443-1446Abstract Full Text Full Text PDF PubMed Scopus (129) Google Scholar). chaperone found in this screen is This protein a of the Lindquist S. J. Biol. Chem. Full Text PDF PubMed Google Scholar). Thus, it is related to both which not influence the [PSI +] propagation, and Hsp70 and which interfered with [PSI +PS] but the [PSI +] curing by excess Hsp104 (10Newnam G.P. Wegrzyn R.D. Lindquist S.L. Chernoff Y.O. 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Cell. 2000; PubMed Scopus Google and could be of and based on these proteins and Sfl1 should with for to thus a of expression in response to different Sfl1 not to the the of the in on Sfl1, being increased both in with excess Sfl1 and in This that Sfl1 has a influence on the factor revealed by [PSI +PS] curing is Ssn8, which a of the transcriptional S. R.D. S. A. 1995; PubMed Scopus Google Scholar). a of and it to and heat as transcriptional and presumably some other chaperone genes EMBO J. 1997; PubMed Scopus Google Scholar). was to with Sfl1 both and functionally. proteins from and both in the transcriptional of M. EMBO J. 1998; PubMed Scopus Google Scholar). 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It is that in to the Sfl1 and different influence on This may that these proteins not in their Although the ribosomal protein Rpp0 is not to participate in we that overproduced Rpp0 increased the and expression which could be sufficient for the [PSI +PS] the the and showed This in the of Rpp0 was at the transcriptional the was the in all that the excess of Rpp0 may by in it either or The is related to the that the lack of acidic ribosomal proteins and and related to affected the expression of many proteins and chaperones in M. A. B. Mol. Cell. Biol. 1995; 15: PubMed Google Scholar). It was that the of acidic proteins in its different It that overproduction of Rpp0 its in it is to that a can more one of this the Rpp0 its overexpression may a of thus a of that lack these in may the of transcriptional factors that the expression of chaperones. properties of yeast prions that they may be used as a model for studying both prions and of (1Wickner R.B. Taylor K.L. Edskes H.K. Maddelein M.L. Moriyama H. Roberts B.T. J. Struct. Biol. 2000; 130: 310-322Crossref PubMed Scopus (67) Google Scholar). This that the factors similar to those found may be and prion and amyloid This is by the that overexpression of Hsp40 and Hsp70 chaperones in interfered with aggregation of proteins with and S.L. J. 1999; 19: PubMed Google Scholar, J. Biol. 2001; PubMed Scopus Google Scholar). In this and previously (9Kushnirov V.V. Kryndushkin D.S. Boguta M. Smirnov V.N. Ter- Avanesyan M.D. Curr. Biol. 2000; 10: 1443-1446Abstract Full Text Full Text PDF PubMed Scopus (129) Google we that the efficiency of the prion curing factors on the prion strain and the of the prion This that the use of based on different prions may finding more factors involved in the prion-like the other this should the of of a factor a given prion or The factors similar to those in this could be prions and chaperones, they of several chaperones of and of for the of and for the and of the
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