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

Overview

Journal J Bacteriol

Publisher American Society for Microbiology

Specialty Microbiology

Date 1973 Sep 1

PMID 4580559

Citations 32

Authors

H Camakaris

J Pittard

Affiliations

Soon will be listed here.

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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