How Big Is the Yeast Prion Universe?

Zhouravleva, Galina A.; Bondarev, Stanislav A.; Trubitsina, Nina P.

doi:10.3390/ijms241411651

Cited by 2 publications

(3 citation statements)

References 116 publications

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“…Primarily, this is because they are prone to either amyloid aggregation or phase separation-based inclusion formation (or both); a number of instances in which they may aid in aggregation of each other have been documented [10,13,54]. Among the Q/N-rich proteins, transcription regulators are frequently found (reviewed in [15]). Several attempts ta screening for such factors affecting the [PSI + ] prion or nonsense suppression have been made; however, these have yielded contradictory results.…”

Section: Discussionmentioning

confidence: 99%

“…These interactions are not limited to only prion-forming proteins; various other Q/N-rich proteins have been shown to act as Pin + -factors [10] as well as to form nonheritable aggregates [13,14] that can indirectly affect prion properties. Notably, transcription factors are often found among Q/N-rich proteins, with at least four of them forming bona fide prions: Ure2, Swi1, Mot3, and Cyc8 (reviewed in [14,15]).…”

Section: Introductionmentioning

confidence: 99%

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Transcription Factors Mcm1 and Sfp1 May Affect [PSI+] Prion Phenotype by Altering the Expression of the SUP35 Gene

Matveenko,

Mikhailichenko,

Drozdova

et al. 2024

Microbiology Research

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Mcm1 is an essential Q/N-rich transcription factor. Q/N-rich proteins interact with each other, and many affect the [PSI+] prion formed by the translation termination factor Sup35 (eRF3). We found that transient MCM1 overexpression increased nonsense suppression in [PSI+] strains and SUP35 transcription. As we had discovered similar effects of another Q/N-rich transcription factor, Sfp1, here we focus on the roles of Mcm1 and Sfp1 in SUP35 expression, as well as on the effects of Sfp1 on the expression of the gene encoding another release factor, Sup45 (eRF1). Mutations in the SUP35 promoter showed that none of the potential Mcm1 binding sites affected the Sup35 protein level or nonsense suppression, even during MCM1 overexpression. Mcm1 itself neither formed aggregates in vivo nor affected Sup35 aggregation. In contrast, a mutation in the Sfp1-binding site decreased Sup35 production and [PSI+] toxicity of excess Sfp1. Mutation of the Sfp1 binding site in the SUP45 promoter lowered SUP45 expression and increased nonsense suppression even more drastically. Our data indicate that the mechanisms of Mcm1 and Sfp1 action differ. While Mcm1 seems unlikely to directly regulate SUP35 expression, Sfp1 appears to act through its binding sites and to directly activate SUP35 expression, which in turn may influence the [PSI+] prion phenotype and toxicity.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Transcription Factors Mcm1 and Sfp1 May Affect [PSI+] Prion Phenotype by Altering the Expression of the SUP35 Gene

Matveenko,

Mikhailichenko,

Drozdova

et al. 2024

Microbiology Research

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“…Currently, about nine yeast amyloid prions are known [ 6 , 7 ]. Two of the best-studied yeast prions are the Sup35 protein, which phenotypically manifests as a nonsense-suppressor [ PSI +] determinant, and the Rnq1 protein, which manifests as a [ PIN +] determinant that greatly enhances the de novo appearance of [ PSI +] and other prions [ 8 ].…”

Section: Introductionmentioning

confidence: 99%

Mapping of Prion Structures in the Yeast Rnq1

Galliamov,

Malukhina,

Kushnirov

2024

IJMS

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The Rnq1 protein is one of the best-studied yeast prions. It has a large potentially prionogenic C-terminal region of about 250 residues. However, a previous study indicated that only 40 C-terminal residues form a prion structure. Here, we mapped the actual and potential prion structures formed by Rnq1 and its variants truncated from the C-terminus in two [RNQ+] strains using partial proteinase K digestion. The location of these structures differed in most cases from previous predictions by several computer algorithms. Some aggregation patterns observed microscopically for the Rnq1 hybrid proteins differed significantly from those previously observed for Sup35 prion aggregates. The transfer of a prion from the full-sized Rnq1 to its truncated versions caused substantial alteration of prion structures. In contrast to the Sup35 and Swi1, the terminal prionogenic region of 72 residues was not able to efficiently co-aggregate with the full-sized Rnq1 prion. GFP fusion to the Rnq1 C-terminus blocked formation of the prion structure at the Rnq1 C-terminus. Thus, the Rnq1-GFP fusion mostly used in previous studies cannot be considered a faithful tool for studying Rnq1 prion properties.

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How Big Is the Yeast Prion Universe?

Cited by 2 publications

References 116 publications

Transcription Factors Mcm1 and Sfp1 May Affect [PSI+] Prion Phenotype by Altering the Expression of the SUP35 Gene

Transcription Factors Mcm1 and Sfp1 May Affect [PSI+] Prion Phenotype by Altering the Expression of the SUP35 Gene

Mapping of Prion Structures in the Yeast Rnq1

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