Neurospora crassa mutant altered in the regulation of L-amino acid oxidase

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 s...

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Published inMicrobiology (Society for General Microbiology) Vol. 143; no. 6; pp. 1969 - 1974
Main Authors Calderon, J, Olvera, L, Martinez, L.M, Davila, G
Format Journal Article
LanguageEnglish
Published Reading Soc General Microbiol 01.06.1997
Society for General Microbiology
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Summary: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; MSO(R) 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 MSO 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 MSO(R) mutation is epistatic to nit-2 since the nit2; MSO(R) double mutant regulated the L-amino acid oxidase in the same way as the MSO(R) single mutant.
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content type line 23
ISSN:1350-0872
1465-2080
DOI:10.1099/00221287-143-6-1969