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- Title
Prion domain interaction responsible for species discrimination in yeast [ PSI<sup>+</sup>] transmission.
- Authors
Hara, Hideyuki; Nakayashiki, Toru; Crist, Colin G.; Nakamura, Yoshikazu
- Abstract
The yeast [ PSI+] factor is transmitted by a prion mechanism involving self-propagating Sup35 aggregates. As with mammalian prions, a species barrier prevents prion transmission between yeast species. The N-terminal of Sup35 of Saccharomyces cerevisiae, necessary for [ PSI+], contains two species-signature elements—a Gln/Asn-rich region (residues 1–41; designated NQ) that is followed by oligopeptide repeats (designated NR). In this study, we show that S. cerevisiae[ PSI+] is transmissible through plasmid shuffling and cytoplasmic transfer to heterotypic Sup35s whose NQ is replaced with the S. cerevisiae NQ. In addition to homology, the N-terminal location is essential for NQ mediated susceptibility to [ PSI+] transmission amongst heterotypic Sup35s. In vitro, a swap of NQ of S. cerevisiae Sup35 led to cross seeding of amyloid formation. These findings suggest that NQ discriminates self from non-self, and is sufficient to initiate [ PSI+] transmission irrespective of whether NR is heterotypic. NR as well as NQ alone coalesces into existing [ PSI+] aggregates, showing their independent potentials to interact with the identical sequence in the [ PSI+] conformer. The role of NQ and NR in [ PSI+] prion formation is discussed.
- Subjects
SACCHAROMYCES cerevisiae; PLASMIDS; CYTOPLASM; NITROGUANIDINE; PRIONS; MEDICAL genetics
- Publication
Genes to Cells, 2003, Vol 8, Issue 12, p925
- ISSN
1356-9597
- Publication type
Article
- DOI
10.1111/j.1365-2443.2003.00694.x