Clearance of yeast prions by misfolded multi-transmembrane proteins.

Accumulation of misfolded proteins in the endoplasmic reticulum (ER) induces the stress response to protect cells against toxicity by the unfolded protein response (UPR), heat shock response (HSR), and ER-associated degradation pathways. Here, we found that over-production of C-terminally truncated multi-transmembrane (MTM) mutant proteins triggers HSR, but not UPR, and clearance of yeast prions [PSI(+)] and [URE3]. One of the mutant MTM proteins, Dip5ΔC-v82, produces a disabled amino-acid permease.

Selfish prion of Rnq1 mutant in yeast.

[PIN(+)] is a prion form of Rnq1 in Saccharomyces cerevisiae and is necessary for the de novo induction of a second prion, [PSI(+)]. We previously isolated a truncated form of Rnq1, named Rnq1Delta100, as a [PSI(+)]-eliminating factor in S. cerevisiae.

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

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.

[Infectious aneurysm rerupture caused by delayed diagnosis: an operative case report].

A 21-year-old febrile woman with sudden onset of headache and semicoma was transferred to our institute. CT and 3D-CT angiography showed subaracnoid hemorrhage and intracranial hemorrhage in the left hemisphere due to a saccular aneurysm at the occluded M2 portion of the middle cerebral artery (MCA). Her present illness started with a toothache and lumber pain 3 weeks earlier.

A regulatory role of the Rnq1 nonprion domain for prion propagation and polyglutamine aggregates.

Prions are infectious, self-propagating protein conformations. Rnq1 is required for the yeast Saccharomyces cerevisiae prion [PIN(+)], which is necessary for the de novo induction of a second prion, [PSI(+)]. Here we isolated a [PSI(+)]-eliminating mutant, Rnq1Delta100, that deletes the nonprion domain of Rnq1.