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. 1973 Sep;115(3):1135–1144. doi: 10.1128/jb.115.3.1135-1144.1973

Regulation of Tyrosine and Phenylalanine Biosynthesis in Escherichia coli K-12: Properties of the tyrR Gene Product

H Camakaris 1, J Pittard 1
PMCID: PMC246363  PMID: 4580559

Abstract

A spontaneous amber tyrR mutant has been isolated in which constitutive synthesis of 3-deoxy-d-arabinoheptulosonic acid 7-phosphate (DAHP) synthetase (tyr) and DAHP synthetase (phe) is suppressible by supC−, supD−, supF− and supU−. This finding suggests the tyrR gene product is a protein. Derepression of DAHP synthetase (phe) in this and in seven other spontaneous tyrR mutants and in four Mu-1-induced tyrR mutants provides further evidence for the involvement of the tyrR gene product in phenylalanine biosynthesis. Evidence that the tyrR product is a component of repressor, rather than an enzyme involved in its synthesis or modification, comes from a study of a temperature-sensitive tyrR mutant. This mutant is of the thermolabile type, since derepression occurs rapidly and in the presence and absence of growth.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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