PMID:15326589

Citation	Gryczynski, U and Schleif, R (2004) A portable allosteric mechanism. Proteins 57:9-11
Abstract	The allosteric mechanism by which the gene expression regulatory protein AraC regulates its DNA-binding activity is shown to be portable by grafting it to beta-galactosidase, generating an arabinose-regulated beta-galactosidase. A portion of the alpha-peptide sequence that complements the activity of alpha-acceptor beta-galactosidase was inserted into a nonessential region of the regulatory peptidyl arm of AraC protein. Arabinose, which regulates the position of the arm in AraC protein now regulates the availability of the alpha-peptide to alpha-acceptor beta-galactosidase, thereby modulating its activity in response to arabinose.
Links	PubMed Online version:10.1002/prot.20233
Keywords	Allosteric Regulation; AraC Transcription Factor; Arabinose/metabolism; Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Escherichia coli/metabolism; Escherichia coli Proteins; Mutagenesis, Site-Directed; Peptide Fragments/chemistry; Peptide Fragments/metabolism; Protein Binding; Recombinant Fusion Proteins/chemistry; Recombinant Fusion Proteins/metabolism; Repressor Proteins/chemistry; Repressor Proteins/metabolism; Structure-Activity Relationship; Transcription Factors/chemistry; Transcription Factors/metabolism; beta-Galactosidase/chemistry; beta-Galactosidase/metabolism
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