Prion-like determinant [NSI +] decreases the expression of the SUP45 gene in Saccharomyces cerevisiae

Kondrashkina, A. M.; Antonets, Kirill S.; Galkin, A. P.; Nizhnikov, Anton A.

doi:10.1134/s0026893314050069

Cited by 8 publications

(6 citation statements)

References 28 publications

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“…Recently, [ SWI + ] has been found to modulate the translation termination efficiency, causing weak translational read-through and omnipotent suppression of the ade1-14 UGA and trp1-289 UAG nonsense alleles [35,37]. This effect only manifests in yeast strains bearing variants of the SUP35 gene encoding the eRF3 release factor [38,39] with decreased functional activity [35,40] and was found to be associated with a decrease of the level of the SUP45 mRNA [41,42] encoding the eRF1 release factor [38,39]. SWI1 deletion also suppresses the phenotype of the ade1-14 UGA mutation [42], but in contrast to [ SWI + ] [41,42], this effect is caused by the increase of the level of the ade1-14 UGA mRNA [43].…”

Section: Introductionmentioning

confidence: 99%

RNA Sequencing Reveals Specific Transcriptomic Signatures Distinguishing Effects of the [SWI+] Prion and SWI1 Deletion in Yeast Saccharomyces cerevisiae

Malovichko

Antonets

Maslova

et al. 2019

Genes

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Prions are infectious, self-perpetuating protein conformers. In mammals, pathological aggregation of the prion protein causes incurable neurodegenerative disorders, while in yeast Saccharomyces cerevisiae, prion formation may be neutral or even beneficial. According to the prevailing contemporary point of view, prion formation is considered to be a functional inactivation of the corresponding protein whose conformational state shifts from the functional monomeric one to the infectious aggregated one. The Swi1 protein forms the [SWI+] prion and belongs to the nucleosome remodeler complex SWI/SNF controlling the expression of a significant part of the yeast genome. In this work, we performed RNA sequencing of isogenic S. cerevisiae strains grown on the media containing galactose as the sole carbon source. These strains bore the [SWI+] prion or had its structural gene SWI1 deleted. The comparative analysis showed that [SWI+] affects genome expression significantly weaker as compared to the SWI1 deletion. Moreover, in contrast to [SWI+], the SWI1 deletion causes the general inhibition of translation-related genes expression and chromosome I disomy. At the same time, the [SWI+] prion exhibits a specific pattern of modulation of the metabolic pathways and some biological processes and functions, as well as the expression of several genes. Thus, the [SWI+] prion only partially corresponds to the loss-of-function of SWI1 and demonstrates several gain-of-function traits.

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Section: Introductionmentioning

confidence: 99%

RNA Sequencing Reveals Specific Transcriptomic Signatures Distinguishing Effects of the [SWI+] Prion and SWI1 Deletion in Yeast Saccharomyces cerevisiae

Malovichko

Antonets

Maslova

et al. 2019

Genes

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“…To date, 12 prions have been identified in Saccharomyces cerevisiae. Of these, 10 are amyloid-based (Kondrashkina et al 2014;Wickner et al 2015). Current models assert that Hsp40-class chaperones, which are cochaperones to Hsp70s, recognize and recruit Hsp70 to the amyloid fibril.…”

Section: Introductionmentioning

confidence: 99%

Three J-proteins impact Hsp104-mediated variant-specific prion elimination: a new critical role for a low-complexity domain

et al. 2019

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Prions are self-propagating protein isoforms that are typically amyloid. In Saccharomyces cerevisiae, amyloid prion aggregates are fragmented by a trio involving three classes of chaperone proteins: Hsp40s, also known as J-proteins, Hsp70s, and Hsp104. Hsp104, the sole Hsp100-class disaggregase in yeast, along with the Hsp70 Ssa and the J-protein Sis1, is required for the propagation of all known amyloid yeast prions. However, when Hsp104 is ectopically overexpressed, only the prion [PSI + ] is efficiently eliminated from cell populations via a highly debated mechanism that also requires Sis1. Recently, we reported roles for two additional J-proteins, Apj1 and Ydj1, in this process. Deletion of Apj1, a J-protein involved in the degradation of sumoylated proteins, partially blocks Hsp104-mediated [PSI + ] elimination. Apj1 and Sis1 were found to have overlapping functions, as overexpression of one compensates for loss of function of the other. In addition, overexpression of Ydj1, the most abundant J-protein in the yeast cytosol, completely blocks Hsp104-mediated curing. Yeast prions exhibit structural polymorphisms known as "variants"; most intriguingly, these J-protein effects were only observed for strong variants, suggesting variant-specific mechanisms. Here, we review these results and present new data resolving the domains of Apj1 responsible, specifically implicating the involvement of Apj1's Q/S-rich low-complexity domain.

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“…Yeast prions are protein-based heritable elements found in the baker's yeast Saccharomyces cerevisiae, of which 12 have been identified to date. 2 Most yeast prions (10 of 12) are formed from amyloid aggregates of normally functional proteins, the 3 best-studied being [PSI C ], [RNQ C ] (often called [PIN C ]), and [URE3]. 3 Amyloid-based prions propagate to daughter cells by cytosolic transfer of small protein aggregates during cell division.…”

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confidence: 99%

Hsp40 function in yeast prion propagation: Amyloid diversity necessitates chaperone functional complexity

Sporn¹,

Hines

2015

Prion

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Yeast prions are heritable protein-based elements, most of which are formed of amyloid aggregates that rely on the action of molecular chaperones for transmission to progeny. Prions can form distinct amyloid structures, known as ‘strains’ in mammalian systems, that dictate both pathological progression and cross-species infection barriers. In yeast these same amyloid structural polymorphisms, called ‘variants’, dictate the intensity of prion-associated phenotypes and stability in mitosis. We recently reported that [PSI+] prion variants differ in the fundamental domain requirements for one chaperone, the Hsp40/J-protein Sis1, which are mutually exclusive between 2 different yeast prions, demonstrating a functional plurality for Sis1.1 Here we extend that analysis to incorporate additional data that collectively support the hypothesis that Sis1 has multiple functional roles that can be accomplished by distinct sets of domains. These functions are differentially required by distinct prions and prion variants. We also present new data regarding Hsp104-mediated prion elimination and show that some Sis1 functions, but not all, are conserved in the human homolog Hdj1/DNAJB1. Importantly, of the 10 amyloid-based prions indentified to date in Saccharomyces cerevisiae, the chaperone requirements of only 4 are known, leaving a great diversity of amyloid structures, and likely modes of amyloid-chaperone interaction, largely unexplored.

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Prion-like determinant [NSI +] decreases the expression of the SUP45 gene in Saccharomyces cerevisiae

Cited by 8 publications

References 28 publications

RNA Sequencing Reveals Specific Transcriptomic Signatures Distinguishing Effects of the [SWI+] Prion and SWI1 Deletion in Yeast Saccharomyces cerevisiae

RNA Sequencing Reveals Specific Transcriptomic Signatures Distinguishing Effects of the [SWI+] Prion and SWI1 Deletion in Yeast Saccharomyces cerevisiae

Three J-proteins impact Hsp104-mediated variant-specific prion elimination: a new critical role for a low-complexity domain

Hsp40 function in yeast prion propagation: Amyloid diversity necessitates chaperone functional complexity

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