PMID:11476551

Citation	Ghosh, M and Schleif, RF (2001) Biophysical evidence of arm-domain interactions in AraC. Anal. Biochem. 295:107-12
Abstract	We report development of a method for the direct measurement of the interaction between the N-terminal arm and the remainder of the dimerization domain in the Escherichia coli AraC protein, the regulator of the l-arabinose operon. The interaction was measured using surface plasmon resonance to monitor the association between the immobilized peptide arm and the dimerization domain, truncated of its arm, in solution. As expected from genetic and physiological data, the interaction is strongly stimulated by l-arabinose and is insensitive to sugars like d-glucose or d-galactose. Alterations in the sequence of the arm which physiological experiments predict either to strengthen or weaken the arm produce the expected responses.
Links	PubMed Online version:10.1006/abio.2001.5213
Keywords	Amino Acid Sequence; AraC Transcription Factor; Arabinose/metabolism; Bacterial Proteins; Biophysical Phenomena; Biophysics; Dimerization; Escherichia coli; Escherichia coli Proteins; Galactose/metabolism; Glucose/metabolism; Molecular Sequence Data; Protein Binding; Protein Structure, Quaternary; Protein Structure, Tertiary; Repressor Proteins/chemistry; Repressor Proteins/metabolism; Surface Plasmon Resonance/methods; Transcription Factors
edit table

Significance

You can help EcoliWiki by summarizing why this paper is useful

You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.

Add links to pages that link here (e.g. gene, product, method pages)

See Help:References for how to manage references in EcoliWiki.