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J. Biol. Chem., Vol. 268, Issue 18, 13023-13025, 06, 1993
J Cui, L Ni and RL Somerville
The TyrR protein of Escherichia coli is the chief transcriptional regulator
of several genes essential for aromatic amino acid biosynthesis and
transport. It was established in previous studies that this protein binds
ATP, that the TyrR.ATP complex has enhanced affinity for tyrosine, and that
the susceptibility of the TyrR protein to hydrolysis by trypsin is altered
by ATP. Here we show that the TyrR protein has ATPase activity, which is
stimulated by tyrosine. In this respect the TyrR protein resembles the
transcriptional activator NtrC. The NtrC protein contains an internal
polypeptide segment, 220 amino acid residues in length, with a high degree
of identity to the TyrR protein, that contains the presumptive ATPase
catalytic center.
ATPase activity of TyrR, a transcriptional regulatory protein for sigma 70 RNA polymerase
Department of Biochemistry, Purdue University, West Lafayette, Indiana 47907.
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