Reference - Detail
| RRC ID | 29917 |
|---|---|
| Author | Camakaris H, Pittard J. |
| Title | Regulation of tyrosine and phenylalanine biosynthesis in Escherichia coli K-12: properties of the tyrR gene product. |
| Journal | J Bacteriol |
| 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. |
| Volume | 115(3) |
| Pages | 1135-44 |
| Published | 1973-9-1 |
| DOI | 10.1128/jb.115.3.1135-1144.1973 |
| PMID | 4580559 |
| PMC | PMC246363 |
| MeSH | Aldehyde-Lyases / biosynthesis Bacterial Proteins* Cell-Free System Coliphages / growth & development Drug Resistance, Microbial Enzyme Repression Escherichia coli / drug effects Escherichia coli / enzymology Escherichia coli / growth & development Escherichia coli / metabolism* Fluorine / pharmacology Genes, Regulator Heptoses Isoenzymes / biosynthesis Lysogeny Mutagens Mutation* Nitrosoguanidines Phenylalanine / biosynthesis* Temperature Tetroses Transduction, Genetic Tyrosine / biosynthesis* Tyrosine / pharmacology |
| IF | 3.006 |
| Resource | |
| Prokaryotes E. coli | ME8604 |