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Papers In Press, published online ahead of print March 28, 2002
J. Biol. Chem, 10.1074/jbc.M112184200
Submitted on December 20, 2001
Revised on March 25, 2002
Accepted on March 28, 2002

The central domain of Escherichia coli TyrR is responsible for hexamerization associated with tyrosine-mediated repression of gene expression

M. P. Dixon, R. N. Pau, G. J. Howlett, D. E. Dunstan, W. H. Sawyer, and B. E. Davidson

Biochemistry and Molecular Biology, The University of Melbourne, Parkville, Victoria 3010

Corresponding Author: r.pau{at}unimelb.edu.au

TyrR from Escherichia coli regulates the expression of genes for aromatic amino acid uptake and biosynthesis. Its central ATP-hydrolysing domain is similar to conserved domains of bacterial regulatory proteins that interact with RNA polymerase holoenzyme associated with the alternative sigma factor, sigma 54. It is also related to the common module of the AAA+ superfamily of proteins that is involved in a wide range of cellular activities. We expressed and purified two TyrR central domain polypeptides. The fragment comprising residues 188 to 467, called TyrR(188-467), was soluble and stable, in contrast to that corresponding to the conserved core from residues 193 to 433. TyrR(188-467) bound ATP and rhodamine-ATP with association constants 2 to 5-fold lower than TyrR and hydrolyzed ATP at five times the rate of TyrR. In contrast to TyrR, which is predominantly dimeric at protein concentrations less than 10 mM in the absence of ligands, or in the presence of ATP or tyrosine alone, TyrR(188-467) is a monomer, even at high protein concentrations. Tyrosine in the presence of ATP or ATPgamma S promotes the oligomerization of TyrR(188-467) to a hexamer. Tyrosine-dependent repression of gene transcription by TyrR therefore depends on ligand binding and hexamerization determinants located in the central domain polypeptide TyrR(188-467).


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