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J. Biol. Chem., Vol. 277, Issue 26, 23186-23192, June 28, 2002
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From the TyrR from Escherichia coli regulates
the expression of genes for aromatic amino acid uptake and
biosynthesis. Its central ATP-hydrolyzing domain is similar to
conserved domains of bacterial regulatory proteins that interact with
RNA polymerase holoenzyme associated with the alternative sigma factor,
In memory of the late Professor Barrie Davidson.
The Central Domain of Escherichia coli TyrR Is
Responsible for Hexamerization Associated with Tyrosine-mediated
Repression of Gene Expression*
§,¶,,
,, and
Department of Biochemistry and Molecular
Biology and the Cooperative Research Centre for Bioproducts,
The University of Melbourne, Parkville 3010, Australia
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 188-467, 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 µM 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 ATP
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).
*
This work was supported by Australian Research Council Large
Grant A09930002 (to B. E. D.).The costs of publication of this article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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