Genetic and metabolic regulation of purine base transport in Neurospora crassa

• Published in: Molecular & general genetics Vol. 149; no. 3; p. 347
• Main Authors: Tsao, T F, Marzluf, G A
• Format: Journal Article
• Language: English
• Published: Germany 01.01.1976
• Subjects: Binding, Competitive; Biological Transport, Active; Genes; Hypoxanthines - metabolism; Kinetics; Neurospora - metabolism; Neurospora crassa - drug effects; Neurospora crassa - metabolism; Purines - metabolism; Purines - pharmacology; Pyrimidines - pharmacology; Uric Acid - metabolism; Xanthines - metabolism
• ISSN: 0026-8925
• DOI: 10.1007/BF00268537

Neurospora crassa can utilize various purine bases such as xanthine or uric acid and their catabolic products as a nitrogen source. The early purine catabolic enzymes in this organism are regulated by induction and by ammonium repression. Studies were undertaken to investigate purine base transport and its regulation in Neurospora. The results of competition experiments with uric acid and xanthine transport strongly suggest that uric acid and xanthine share a common transport system. It was also shown that the common transport system for uric acid and xanthine is distinct from a second transport system shared by hypoxanthine, adenine and guanine, and apparently also distinct from the transport system(s) for adenosine, cytosine and uracil. Regulation of the uric acid-xanthine transport system and the hypoxanthine-adenine-guanine transport system was studied. The results reveal that the uric acid-xanthine transport system is regulated by ammonium repression, but does not require uric acid induction. Neither ammonium repression nor uric acid induction controls the hypoxanthine-adenine-guanine transport system. A gene, designated amr, which is believed to be a positive regulatory gene for nitrogen metabolism of Neurospora crassa, was found to dramatically affect both the uric acid-xanthine transport system and the hypoxanthine-adenine-guanine transport system. A model for the action of the amr locus as a positive regulatory gene and for the interaction between the amr gene product and its recognition sites will be discussed.