Ure2p Function Is Enhanced by Its Prion Domain in Saccharomyces cerevisiae

• DOI: 10.1534/genetics.107.074153
• Publication Date: 2007-05-17T01:11:03Z
• Authors: Frank Shewmaker; Lori Mull; Toru Nakayashiki; Daniel C Masison; Reed B Wickner
• Keywords: Glutathione Peroxidase; 0303 health sciences; 03 medical and health sciences; Saccharomyces cerevisiae Proteins; Codon, Nonsense; Nitrogen; Prions; GATA Transcription Factors; Protein Structure, Tertiary

The Ure2 protein of Saccharomyces cerevisiae can become a prion (infectious protein). At very low frequencies Ure2p forms an insoluble, infectious amyloid known as [URE3], which is efficiently transmitted to progeny cells or mating partners that consequently lose the normal nitrogen regulatory function. [URE3] causes yeast grow slowly, has never been identified in wild, and confers no obvious phenotypic advantage. An N-terminal asparagine-rich domain determines prion-forming ability. Since ure2Delta strains are complemented by plasmids overexpress truncated lacking domain, existence evolutionary conservation extension have remained mysteries. We find function actually compromised vivo truncation domain. Moreover, stability diminished without full-length Mca1p, like Ure2p, Q/N-rich whose deletion reduces its steady-state levels. Finally, we demonstrate may affect interaction with other components regulation system, specifically negative regulator catabolic genes, Gzf3p.