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M008705200v1
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Papers In Press, published online ahead of print November 7, 2000
J. Biol. Chem, 10.1074/jbc.M008705200
Submitted on September 22, 2000
Revised on October 30, 2000
Accepted on November 7, 2000

Strengthened arm-dimerization domain interactions in AraC

Martin Wu and Robert Schleif

Department of Biology, Johns Hopkins University, Baltimore, MD 21218

Corresponding Author: bob{at}gene.bio.jhu.edu

Constitutive mutations were sought and found in the N-terminal arm of the Escherichia coli regulatory protein of the arabinose operon, AraC protein. A new mutation, N16D, was of particular interest. N16 is not seen in the crystal structure of the AraC dimerization domain determined in the absence of arabinose because the N-terminal arm 18 residues are disordered, but in the presence of arabinose, residues 7-18 fold over the arabinose and make many interactions with it. In this state N16 lies near two positively charged amino acids, K43 and R99. We propose that the introduction of the negatively charged aspartic residue at position 16 creates a charge-charge interaction network among D16, K43, and R99 that holds the arm to the dimerization domain even in the absence of arabinose. This frees the DNA-binding domains and allows them to bind cis to I1-I2 half-sites and activate transcription. Mutating the two positively charged residues to alanines individually and collectively decreased or eliminated the constitutivity created by the N16D mutation.


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