IS2 activates the ilvA gene of Pseudomonas cepacia in Escherichia coli.
AUTOR(ES)
Barsomian, G
RESUMO
The ilvA gene of Pseudomonas cepacia was expressed poorly in Escherichia coli. Insertion of IS2 upstream of the cloned gene dramatically increased its transcription, resulting in an 85-fold increase in threonine dehydratase (deaminase) specific activity. The results confirm earlier reports that IS2 promotes efficient expression of foreign genes in E. coli.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=212018Documentos Relacionados
- Translational coupling between the ilvD and ilvA genes of Escherichia coli.
- Complementation Between Different Mutations in the ilvA Gene of Escherichia coli K-12
- An efficient approach to identify ilvA mutations reveals an amino-terminal catalytic domain in biosynthetic threonine deaminase from Escherichia coli.
- Multivalent regulation of isoleucine-valine transaminase in an Escherichia coli K-12 ilvA deletion strain.
- Transcription initiation sites within an IS2 insertion in a Gal-constitutive mutant of Escherichia coli.