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PMID: 4580559 Published · ppublish English Journal Article

Regulation of tyrosine and phenylalanine biosynthesis in Escherichia coli K-12: properties of the tyrR gene product.

Journal of bacteriology ·Vol. 115 ·No. 3 ·1973-09-00 ·Pages 1135-44

Camakaris H, Pittard J

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.

MeSH Terms
Aldehyde-Lyases/biosynthesis Bacterial Proteins Cell-Free System Coliphages/growth & development Drug Resistance, Microbial Enzyme Repression Escherichia coli/drug effects,enzymology,growth & development,metabolism Fluorine/pharmacology Genes, Regulator Heptoses Isoenzymes/biosynthesis Lysogeny Mutagens Mutation Nitrosoguanidines Phenylalanine/biosynthesis Temperature Tetroses Transduction, Genetic Tyrosine/biosynthesis,pharmacology
Chemicals
Bacterial Proteins Heptoses Isoenzymes Mutagens Nitrosoguanidines Tetroses Fluorine Tyrosine Phenylalanine Aldehyde-Lyases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Camakaris H
Pittard J
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31 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
DOI
10.1128/jb.115.3.1135-1144.1973
Published
1973-09-00
Pages
1135-44
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC246363
Subset
IM
External Links
PubMed source DOI: 10.1128/jb.115.3.1135-1144.1973 PMC Full Text View journal details
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