Construction of an effective protein expression system using the tpl promoter in Escherichia coli.
An effective protein expression system was constructed in Escherichia coli using the promoter of the tyrosine phenol-lyase (tpl) gene of Erwinia herbicola. This system involves a mutant form of the TyrR protein with an enhanced ability to activate tpl and the TutB protein with an ability to transport L-tyrosine (an inducer of Tpl). The highest expression level obtained for this system was more than twice that obtained for the tac system, although it was lower than the level obtained for the T7 system, as revealed with the lac-reporter assay and SDS-polyacrylamide gel electrophoresis.
Koyanagi
Takashi
T
Division of Integrated Life Science, Graduate School of Biostudies, Kyoto University, Sakyo-ku Kyoto, 606-8502, Japan.
Katayama
Takane
T
Hirao
Ai
A
Suzuki
Hideyuki
H
Kumagai
Hidehiko
H
D026921:Amino Acid Transport Systems, Neutral / Q000235:genetics*; D004926:Escherichia coli / Q000235:genetics*; D029968:Escherichia coli Proteins / Q000235:genetics*; D015964:Gene Expression Regulation, Bacterial / Q000235:genetics*; D009154:Mutation; D011401:Promoter Regions, Genetic; D012097:Repressor Proteins / Q000235:genetics*; D014447:Tyrosine Phenol-Lyase / Q000235:genetics*
D026921:Amino Acid Transport Systems, Neutral; D029968:Escherichia coli Proteins; D012097:Repressor Proteins; C069256:TyrR protein, E coli; D014447:Tyrosine Phenol-Lyase