araC Antibody

1. Arabinose binding to the AraC dimerization domain changes the properties of the AraC inter-domain linker which connects the dimerization domain to the DNA binding domain via interactions that do not depend on the DNA binding domain. PMID: 26800223
2. Data [including data from studies of mutant AraC (P8G, P8A)] suggest that, in AraC conformation, interaction of the N-terminal arm with something other than the front lip is the primary determinant of the inducing versus repressing state of AraC. PMID: 25243377
3. Interaction between domains of AraC in presence of arabinose is reported. Dissociation of arabinose-bound AraC from half-site DNA is faster than free DNA binding domain;affinity of dimeriz'n domains for arabinose is increased when half-site DNA is bound. PMID: 22383259
4. Mutation in the interdomain affect the dimerization domain-DNA-binding domain interactions in AraC. PMID: 21840981
5. The allosteric mechanism by which the gene expression regulatory protein AraC regulates its DNA-binding activity is shown to be portable. PMID: 15326589
6. Apparently, interactions between the N-terminal arm and the dimerization domain core position the arm to interfere with the protein-protein contacts necessary for self-association. PMID: 17132863
7. The majority of the constitutive mutations lie within the same residues of the N-terminal regulatory arm of AraC. Two, however, were found in the core of the dimerization domain. PMID: 19218388

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KEGG: ecj:JW0063

STRING: 316407.21321946