In Vitro Synthesis of Enzymes of the Tryptophan Operon of Escherichia coli
AUTOR(ES)
Pouwels, P. H.
RESUMO
Two active enzymes of the tryptophan operon of E. coli, anthranilate synthetase (product of trp E and trp D) and tryptophan synthetase (EC 4.2.1.20) (product of trp B and trp A), have been synthesized in a DNA-dependent preparation for protein synthesis. Anthranilate synthetase and the two components of tryptophan synthetase (tryptophan synthetase A and B) are made in vitro in equimolar amounts, suggesting that regulation of the translation is similar in vivo and in vitro. Kinetics of the synthesis of the two enzymes suggest that transcription and translation proceed in vitro in a correct temporal sequence.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=426802Documentos Relacionados
- Escherichia coli mutant strain with altered expression of the tryptophan operon: ribonucleic acid synthesis in vitro.
- In vitro synthesis of the tryptophan operon leader peptides of Escherichia coli, Serratia marcescens, and Salmonella typhimurium.
- Escherichia coli tryptophan operon directs the in vivo synthesis of a leader peptide.
- Temperature-sensitive Repression of the Tryptophan Operon in Escherichia coli
- Tandem termination sites in the tryptophan operon of Escherichia coli.
