Nitrogen catabolite repression regulator Ure2 (Ure2)

Nitrogen catabolite repression regulator Ure2 (Ure2p) is a multifunctional protein found in the yeast Saccharomyces cerevisiae that serves as a master regulator of nitrogen metabolism. It functions by binding and sequestering GATA-type transcription factors, such as Gln3 and Gat1, in the cytoplasm to prevent the expression of genes involved in utilizing poor nitrogen sources when preferred sources like ammonia or glutamine are available. Ure2 is structurally characterized by a disordered N-terminal prion domain and a C-terminal domain with homology to glutathione S-transferases (GSTs), which provides cellular protection against oxidative stress and heavy metal toxicity. The protein is highly significant in biomedical research as the molecular determinant of the [URE3] prion, a self-propagating amyloid state that leads to the loss of its regulatory function. While not a direct human therapeutic target, Ure2 is extensively utilized as a biological model to study the mechanisms of protein misfolding, amyloidogenesis, and prion inheritance, providing insights into human neurodegenerative diseases like Alzheimer's and Parkinson's. Experimental inhibitors such as epigallocatechin gallate (EGCG) and chemical chaperones are often tested against Ure2 to explore strategies for preventing amyloid formation.

Other names

Ure2pProtein URE2Glutathione S-transferase Ure2[URE3]Transcriptional regulator URE2

Experimental inhibition of amyloid aggregation and prion propagation; modulation of GATA transcription factor localization.