{'fraction_non_alphanumeric': 0.019444444444444445, 'fraction_numerical': 0.007407407407407408, 'mean_word_length': 5.358823529411764, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
A new and unexpected domain–domain interaction in the AraC protein

An interaction between the dimerization domains and DNA binding domains of the dimeric AraC protein has previously been shown to facilitate repression of the Escherichia coli araBAD operon by AraC in the absence of arabinose. A new interaction between the domains of AraC in the presence of arabinose is reported here, the regulatory consequences of which are unknown. Evidence for the interaction is the following: the dissociation rate of arabinose‐bound AraC from half‐site DNA is considerably faster than that of free DNA binding domain, and the affinity of the dimerization domains for arabinose is increased when half‐site DNA is bound. In addition, an increase in the fluorescence intensity of tryptophan residues located in the arabinose‐bound dimerization domain is observed upon binding of half‐site DNA to the DNA binding domains. Direct physical evidence of the new domain–domain interaction is demonstrated by chemical crosslinking and NMR experiments. Proteins 2012;. © 2012 Wiley Periodicals, Inc.