Abstract
J Calderon, L Olvera, LM Martinez and G Davila
Departamento de Biotecnologia, Instituto de Investigaciones Biomedicas, Universidad Nacional Autonoma de Mexico, Mexico DF, Mexico. JFCJ@SERVIDOR.UNAM.MX
The isolation and characterization of a Neurospora crassa mutant altered in L-amino oxidase regulation is reported. The previously isolated gln-1bR8 strain, which only synthesizes the glutamine synthetase alpha monomer and lacks the beta monomer, was used as parental strain. A mutant derivative of strain was selected for its ability to grow on minimal medium in the presence of DL-methionine-SR- sulfoximine (MSO), an inhibitor of glutamine synthetase activity. This gln-1bR8;MSOR mutant overcame the inhibitory effect of MSO by increasing the activity of L-amino acid oxidase, an enzyme capable of degrading this compound. In contrast with the wild-type strain, the L- amino acid oxidase of the MSOR mutant was resistant to glutamine repression; in fact, it was induced by this amino acid but repressed by ammonium. This mutant is different from other nitrogen regulatory N. crassa mutants reported and is only altered in the regulation of L- amino acid oxidase. The MSOR mutation is epistatic to nit-2 since the nit2;MSOR double mutant regulated the L-amino acid oxidase in the same way as the MSOR single mutant.