A bipolar personality of yeast prion proteins

作者：Kurahashi Hiroshi; Oishi Keita; Nakamura Yoshikazu^*

来源：Prion, 2011, 5(4): 305-310.

DOI：10.4161/pri.5.4.18307

• yeast prion
• [PSI+]
• Pin(+)
• [RNQ(+)]
• [RNQ1 Delta 100(+)]
• [URE3]
• Lsm4
• New1

Prions are infectious, self-propagating protein conformations. [PSI+], [RNQ(+)] and [URE3] are well characterized prions in Saccharomyces cerevisiae and represent the aggregated states of the translation termination factor Sup35, a functionally unknown protein Rnq1 and a regulator of nitrogen metabolism Ure2, respectively. Overproduction of Sup35 induces the de novo appearance of the [PSI+] prion in [RNQ(+)] or [URE3] strain, but not in non-prion strain. However, [RNQ(+)] and [URE3] prions themselves, as well as overexpression of a mutant Rnq1 protein, Rnq1 Delta 100 and Lsm4, hamper the maintenance of [PSI+]. These findings point to a bipolar activity of [RNQ(+)], [URE3], Rnq1 Delta 100 and Lsm4, and probably other yeast prion proteins as well, for the fate of [PSI+] prion. Possible mechanisms underlying the apparent bipolar activity of yeast prions will be discussed.

• 出版日期2011-12
• 单位河北医科大学