PMID:8516313
| Citation |
Bustos, SA and Schleif, RF (1993) Functional domains of the AraC protein. Proc. Natl. Acad. Sci. U.S.A. 90:5638-42 |
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| Abstract |
The AraC protein, which regulates the L-arabinose operons in Escherichia coli, was dissected into two domains that function in chimeric proteins. One provides a dimerization capability and binds the ligand arabinose, and the other provides a site-specific DNA-binding capability and activates transcription. In vivo and in vitro experiments showed that a fusion protein consisting of the N-terminal half of the AraC protein and the DNA-binding domain of the LexA repressor dimerizes, binds well to a LexA operator, and represses expression of a LexA operator-beta-galactosidase fusion gene in an arabinose-responsive manner. In vivo and in vitro experiments also showed that a fusion protein consisting of the C-terminal half of the AraC protein and the leucine zipper dimerization domain from the C/EBP transcriptional activator binds to araI and activates transcription from a PBAD promoter-beta-galactosidase fusion gene. Dimerization was necessary for occupancy and activation of the wild-type AraC binding site. |
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| Keywords |
AraC Transcription Factor; Arabinose/metabolism; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Cloning, Molecular; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins; Kinetics; Operon; Polymerase Chain Reaction; Promoter Regions, Genetic; Recombinant Fusion Proteins/metabolism; Repressor Proteins/genetics; Repressor Proteins/metabolism; Restriction Mapping; Serine Endopeptidases; Transcription Factors; beta-Galactosidase/genetics; beta-Galactosidase/metabolism |
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