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Aromatic amino acid biosynthesis and para-fluorophenylalanine resistance in Aspergillus nidulans

Published online by Cambridge University Press:  14 April 2009

Umakant Sinha
Umakant Sinha
Affiliation:
Department of Genetics, University of Glasgow
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1. Five additional phenylalanine (PHE)-requiring mutants have been isolated but they do not add to the number of loci already known which have been designated phenA (phen2 and its alleles) and phenB (phen6).

2. Two pathways for tyrosine (TYR) synthesis in A. nidulans have been proposed: the well-known one by the transamination of p-hydroxyphenylpyruvic acid and an alternative one, as in animals, by the hydroxylation of PHE.

3. Ten allelic partial TYR-requiring mutants (tyrA), presumably blocked in the transamination pathway, have been isolated after N-methyl-N′-nitro-N-nitrosoguanidine (NTG) treatment of bil;phenA3 conidia.

4. Four partial TYR requirers (at another locus—tyrB) have been isolated after NTG treatment of tyr A7, bi1 conidia. They are presumably blocked in an alternative pathway for TYR synthesis, i.e. in the PHE-hydroxylation pathway.

5. tyrA mutants have been found to be p-fluorophenylalanine (FPA)-resistant and allelic to mutants at the fpA locus. tyrB mutants have been found to be very leaky and FPA-sensitive. tyrA;tyrB double mutants have been found to be exacting TYR requirers.

6. Mutants at loci fpA (tyrA) and fpE (anthranilic acid-requiring) have been interpreted to be p-fluorophenylalanine-resistant due to an oversynthesis of PHE.

Type
Research Article
Information
Genetics Research , Volume 10 , Issue 3 , December 1967 , pp. 261 - 272
Copyright
Copyright © Cambridge University Press 1967

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