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J Biol Chem, Vol. 274, Issue 38, 26727-26735, September 17, 1999
From the Department of Molecular and Cell Biology, Division of
Biochemistry and Molecular Biology, University of California,
Berkeley, California 94720-3202
The membrane-bound complex of the
Salmonella typhimurium histidine permease, a member of the
ABC transporters (or traffic ATPases) superfamily, is composed of two
integral membrane proteins, HisQ and HisM, and two copies of an
ATP-binding subunit, HisP, which hydrolyze ATP, thus supplying the
energy for translocation. The three-dimensional structure of HisP has
been resolved. Extensive evidence indicates that the HisP subunits form
a dimer. We investigated the mechanism of action of such a dimer, both
within the complex and in soluble form, by creating heterodimers
between the wild type and mutant HisP proteins. The data strongly
suggest that within the complex both subunits hydrolyze ATP and that
one subunit is activated by the other. In a heterodimer containing one
wild type and one hydrolysis defective subunit both hydrolysis and ligand translocation occur at half the rate of the wild type. Soluble
HisP also hydrolyzes ATP if one subunit is inactive; its specific
activity is identical to that of the wild type, indicating that only
one of the subunits in a soluble dimer is involved in hydrolysis. We
show that the activating ability varies depending on the nature of the
substitution of a well conserved residue, His-211.
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