Selfish prion of Rnq1 mutant in yeast

Kurahashi, Hiroshi; Shibata, Shoichiro; Ishiwata, Masao; Nakamura, Yoshikazu

doi:10.1111/j.1365-2443.2009.01297.x

Cited by 12 publications

(14 citation statements)

References 23 publications

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“…However, a deletion mutant of N‐terminal nonprion domain (amino acids 1–100), Rnq1Δ100, shows several intriguing properties. First, Rnq1Δ100 is capable of forming and transmitting the [ PIN + ] prion in accordance with the aforementioned findings (Kurahashi et al. 2009).…”

Section: Introductionsupporting

confidence: 81%

[PSI+] aggregate enlargement in rnq1 nonprion domain mutants, leading to a loss of prion in yeast

et al. 2011

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Section: Introductionsupporting

confidence: 81%

[PSI+] aggregate enlargement in rnq1 nonprion domain mutants, leading to a loss of prion in yeast

et al. 2011

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“…They report curing of one or several yeast prions ([ URE3 ] and, sometimes, [ PSI + ] or [ PIN + ]) by overexpression of Gpg1, a non-Q/N-rich G-protein γ-subunit mimic 42 ; by overexpression of mutant alleles of Rnq1 in [ PIN + ] strains; and by a Rnq1-Δ100 deletion or an array of rnq1 point mutations in the presence of [ PIN + ] 20 - 22 , 43 . Also, overexpression of two more proteins identified in our screen for [ PIN + ], 12 Lsm4 and New1, was recently shown to cause cells to lose prions 44 , 45 .…”

Section: Other Negative Prion-prion Interactions: Applicability Of Timentioning

confidence: 99%

“…They include mutual inhibition and destabilization of co-existing prions, and inhibition of de novo prion appearance by a pre-existing prion 18 - 20 . Also, [ PSI + ] and [ URE3 ] can be cured by overexpression of Rnq1 deletion or point mutants in the presence of [ PIN + ], and overexpression of GFP-tagged Ure2 fragments capable of inducing the [ URE3 ] prion can cure pre-existing [ URE3 ] 21 - 24 …”

mentioning

confidence: 99%

The story of stolen chaperones

Derkatch

Liebman

2013

Prion

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Prions are self-seeding alternate protein conformations. Most yeast prions contain glutamine/asparagine (Q/N)-rich domains that promote the formation of amyloid-like prion aggregates. Chaperones, including Hsp104 and Sis1, are required to continually break these aggregates into smaller “seeds.” Decreasing aggregate size and increasing the number of growing aggregate ends facilitates both aggregate transmission and growth. Our previous work showed that overexpression of 11 proteins with Q/N-rich domains facilitates the de novo aggregation of Sup35 into the [PSI+] prion, presumably by a cross-seeding mechanism. We now discuss our recent paper, in which we showed that overexpression of most of these same 11 Q/N-rich proteins, including Pin4C and Cyc8, destabilized pre-existing Q/N rich prions. Overexpression of both Pin4C and Cyc8 caused [PSI+] aggregates to enlarge. This is incompatible with a previously proposed “capping” model where the overexpressed Q/N-rich protein poisons, or “caps,” the growing aggregate ends. Rather the data match what is expected of a reduction in prion severing by chaperones. Indeed, while Pin4C overexpression does not alter chaperone levels, Pin4C aggregates sequester chaperones away from the prion aggregates. Cyc8 overexpression cures [PSI+] by inducing an increase in Hsp104 levels, as excess Hsp104 binds to [PSI+] aggregates in a way that blocks their shearing.

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“…33 Furthermore, prions of Rnq1Δ100 and the Rnq1 missense mutant proteins are unstable under their native expression levels but are stable when overexpressed. 31,32 Therefore, Rnq1Δ100 and the missense mutant proteins share the phenotype. These findings strongly suggest that these N-terminal nonprion-domain mutants exhibit the same activity as Rnq1Δ100.…”

Section: A Bipolar Activity Of Lsm4mentioning

confidence: 99%