The glutamine - and asparagine-rich protein, Rnq1, is a putative yeast prion. Rnq1 protein with yet unknown function, can exists in either noninfectious soluble monomer form, [pin-], or the insoluble aggregated amyloid-like form called [PIN+]. The insoluble state is dominant and transmitted between cells through the cytoplasm (1). Rnq1 protein is necessary for the de novo induction of another prion, [PSI+] (2). The molecular chaperone Hsp104 is necessary for the aggregate formation of polyglutamine and for the maintenance of prion phenotype. The pre-existing aggregates are required for the chaperon-dependent establishment of the epigenetic trait in yeast prions (3).
Data Link SGD RNQ1/YCL028W
1) Western blotting (x 300 fold dilution)
2) Not tested for other applications.
Cells were harvested after 24 h of galactose induction. Extracts were centrifuged and soluble (S) and pelleted (P) fractions were assayed by Western blotting using this antibody.
Rnq1 protein was detected in pelleted fraction (ref. 3).
< Reference >
1. Sondheimer, N. & Lindquist, S. “Rnq1: an epigenetic modifier of protein function in yeast” Mol Cell 5, 163-172 (2000) PMID: 10678178
2. Derkatch, I.L. et al. “Effects of Q/N-rich, polyQ, and non-polyQ amyloids on the de novo formation of the [PSI+] prion in yeast and aggregation of Sup35 in vitro.” Proc. Natl. Acad. Sci. USA. 101,
12934-12939 (2004) PMID: 15326312
3. Kimura,Y. et al. “The role of pre-existing aggregates in Hsp104 - dependent polyglutamine aggregate formation and epigenetic change of yeast prions.” Genes to Cells 9, 685-696 (2004) PMID: 15298677