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J Biol Chem, Vol. 274, Issue 26, 18310-18318, June 25, 1999
From the Department of Molecular and Cell Biology, University of
California, Berkeley, California 94720
The membrane-bound complex of the prokaryotic
histidine permease, a periplasmic protein-dependent ABC
transporter, is composed of two hydrophobic subunits, HisQ and HisM,
and two identical ATP-binding subunits, HisP, and is energized by ATP
hydrolysis. The soluble periplasmic binding protein, HisJ, creates a
signal that induces ATP hydrolysis by HisP. The crystal structure of HisP has been resolved and shown to have an "L" shape, with one of
its arms (arm I) being involved in ATP binding and the other one (arm
II) being proposed to interact with the hydrophobic subunits (Hung,
L.-W., Wang, I. X., Nikaido, K., Liu, P.-Q., Ames, G. F.-L., and Kim, S.-H. (1998) Nature 396, 703-707). Here we study
the basis for the defect of several HisP mutants that have an altered signaling pathway and hydrolyze ATP constitutively. We use biochemical approaches to show that they produce a loosely assembled membrane complex, in which the mutant HisP subunits are disengaged from HisQ and
HisM, suggesting that the residues involved are important in the
interaction between HisP and the hydrophobic subunits. In addition, the
mutant HisPs are shown to have lower affinity for ADP and to display no
cooperativity for ATP. All of the residues affected in these HisP
mutants are located in arm II of the crystal structure of HisP, thus
supporting the proposed function of arm II of HisP as interacting with
HisQ and HisM. A revised model involving a cycle of disengagement and
reengagement of HisP is proposed as a general mechanism of action for
ABC transporters.
Modulation of ATPase Activity by Physical Disengagement of the
ATP-binding Domains of an ABC Transporter, the Histidine
Permease
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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