A G-protein gamma subunit mimic is a general antagonist of prion propagation in Saccharomyces cerevisiae.

Proceedings of the National Academy of Sciences of the United States of America
Masao IshiwataYoshikazu Nakamura

Abstract

The Gpg1 protein is a Ggamma subunit mimic implicated in the G-protein glucose-signaling pathway in Saccharomyces cerevisiae, and its function is largely unknown. Here we report that Gpg1 blocks the maintenance of [PSI(+)], an aggregated prion form of the translation termination factor Sup35. Although the GPG1 gene is normally not expressed, over-expression of GPG1 inhibits propagation of not only [PSI(+)] but also [PIN(+)], [URE3] prions, and the toxic polyglutamine aggregate in S. cerevisiae. Over-expression of Gpg1 does not affect expression and activity of Hsp104, a protein-remodeling factor required for prion propagation, showing that Gpg1 does not target Hsp104 directly. Nevertheless, prion elimination by Gpg1 is weakened by over-expression of Hsp104. Importantly, Gpg1 protein is prone to self-aggregate and transiently colocalized with Sup35NM-prion aggregates when expressed in [PSI(+)] cells. Genetic selection and characterization of loss-of-activity gpg1 mutations revealed that multiple mutations on the hydrophobic one-side surface of predicted alpha-helices of the Gpg1 protein hampered the activity. Prion elimination by Gpg1 is unaffected in the gpa2Delta and gpb1Delta strains lacking the supposed physiological G-prote...Continue Reading

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Citations

Apr 25, 2012·The Journal of Cell Biology·Sebastian Treusch, Susan Lindquist
Apr 18, 2009·Genes to Cells : Devoted to Molecular & Cellular Mechanisms·Hiroshi KurahashiYoshikazu Nakamura
Apr 2, 2011·Genes to Cells : Devoted to Molecular & Cellular Mechanisms·Hiroshi KurahashiYoshikazu Nakamura
Mar 21, 2013·MicrobiologyOpen·Keita OishiYoshikazu Nakamura

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