期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：2010
卷号：107
期号：23
页码：10573-10577
DOI：10.1073/pnas.1005949107
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Four protein-based genetic determinants or prions--[SWI+], [MCA], [OCT+], and [MOT3+]--are recent additions to the list of well-known Saccharomyces cerevisiae prions, [PSI+], [URE3], and [PIN+]. A rapid expansion of this list may indicate that many yeast proteins can convert into heritable prion forms and underscores a problem of prion input into cellular physiology. Here, we prove that the global transcriptional regulator Sfp1 can become a prion corresponding to the prion-like determinant [ISP+] described earlier. We show that SFP1 deletion causes an irreversible [ISP+] loss, whereas increased SFP1 expression induces [ISP+] appearance. Cells that display the [ISP+] phenotype contain the aggregated form of Sfp1. Indeed, these aggregates demonstrate a nuclear location. We also show that the phenotypic manifestation of Sfp1 prionization differs from the manifestation of SFP1 deletion. These properties and others distinguish [ISP+] from yeast prions described to date.
