The regulation of urease activity in Aspergillus nidulans.
Aspergillus nidulans can utilize urea as a sole source of nitrogen but not as a carbon source. Urea is degraded by a urease. Mutation at any one of three genes, ureB, ureC, and ureD, may result in deficient urease activity. The ureB gene is closely linked to ureA, the structural gene for the urea transport protein. The heat lability of ureB- revertant strain, intragenic complementation tests, and the linkage of ureB to ureA suggest that ureB is the urease structural gene. The ureD gene is probably involved in the synthesis or incorporation of a nickel cofactor essential for urease activity. The function of the ureC gene is not known. Urease is not induced but is subject to nitrogen regulation. The urease activities of ammonium-derepressed mutants show that the effector of nitrogen regulation is more likely to be glutamine than ammonium. When glutamine is present in the medium, urease appears to be inactivated by some means which does not involve a newly synthesized protease or a direct interaction between glutamine and urease.
D001233:Aspergillus nidulans / Q000201:enzymology / Q000235:genetics*; D003513:Cycloheximide / Q000494:pharmacology; D005786:Gene Expression Regulation / Q000187:drug effects; D005816:Genetic Complementation Test; D008040:Genetic Linkage; D006639:Histidine / Q000494:pharmacology; D009532:Nickel / Q000494:pharmacology; D009584:Nitrogen / Q000494:pharmacology; D013696:Temperature; D014510:Urease / Q000235:genetics*
D006639:Histidine; D009532:Nickel; D003513:Cycloheximide; D014510:Urease; D009584:Nitrogen