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Mutants affecting amino acid cross-pathway control in Neurospora crassa

Published online by Cambridge University Press:  14 April 2009

Ilse B. Barthelmess
Affiliation:
Institut für Angewandte Genetik, Universität Hannover, D 3000 Hannover, Federal Republic of Germany
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Summary

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Arginine-requiring mutants of Neurospora crassa were isolated using a strain partially impaired in an enzyme of the arginine pathway (bradytroph). Among these, five strains were found which carry mutations at a new locus, cpc-1+. The recessive cpc-1 alleles interfere with the cross-pathway control of amino acid biosynthetic enzymes. The enzymes studied, three of arginine and one each of histidine and lysine biosynthesis, fail to derepress under conditions which normally result in elevation of enzyme concentration, namely arginine, histidine or tryptophan limitation. Enzymes not involved in amino acid biosynthesis are still able to derepress in the presence of cpc-1. In wild-type backgound, i.e. with the bradytroph replaced, cpc-1 strains lose the original arginine-requirement. cpc-1 mutations confer sensitivity of growth to 3-amino-1,2,4-triazole.

Type
Research Article
Copyright
Copyright © Cambridge University Press 1982

References

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