Repression of the tyrosine, lysine, and methionine biosynthetic pathways in a hisT mutant of Salmonella typhimurium.
AUTOR(ES)
Brown, B A
RESUMO
A comparison was made of the repressibility of certain enzymes in the tyrosine, methionine, and lysine biosynthetic pathways in wild-type Salmonella typhimurium and a hisT mutant. The results show that (i) tyrosine represses the synthesis of the tyrosine-sensitive 3-deoxy-D-arabino-heptulsonic acid 7-phosphate synthetase and the tyrosine aminotransferase to the same extent in a hisT mutant as in wild type and (ii) there is no detectable alteration in the extent to which methionine represses O-succinylhomoserine synthetase or in the extent to which lysine represses the lysine-sensitive beta-aspartokinase as a result of the hisT mutation.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=235064Documentos Relacionados
- Regulation of nitrogen utilization of hisT mutants of Salmonella typhimurium.
- Histidine Regulation in Salmonella typhimurium VIII. Mutations of the hisT Gene
- Interaction between phosphoribosyltransferase and purified histidine tRNA from wild type Salmonella typhimurium and a derepressed hisT mutant strain.
- Effects of the hisT mutation of Salmonella typhimurium on translation elongation rate.
- Characterization of a cold-sensitive hisW mutant of Salmonella typhimurium.
