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J. Biol. Chem., Vol. 277, Issue 24, 21111-21114, June 14, 2002
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From the Departments of ATP-binding cassette (ABC)
transporters harvest the energy present in cellular ATP to drive the
translocation of a structurally diverse set of solutes across the
membrane barriers of eubacteria, archaebacteria, and eukaryotes. The
positively cooperative ATPase activity (Hill coefficient, 1.7) of a
model soluble cassette of known structure, MJ0796, from
Methanococcus jannaschii indicates that at least two
binding sites participate in the catalytic reaction. Mutation of the
catalytic base in MJ0796, E171Q, produced a cassette that can bind but
not efficiently hydrolyze ATP. The equivalent mutation (E179Q) in a
homologous cassette, MJ1267, had an identical effect. Both mutant
cassettes formed dimers in the presence of ATP but not ADP, indicating
that the energy of ATP binding is first coupled to the transport cycle
through a domain association reaction. The non-hydrolyzable nucleotides
adenosine 5'-(
ACCELERATED PUBLICATION
Cooperative, ATP-dependent Association
of the Nucleotide Binding Cassettes during the Catalytic
Cycle of ATP-binding Cassette Transporters*
§,§,
, and**
Physiology and
¶ Pharmacology, The University of Texas Southwestern Medical
Center, Dallas, Texas 75390-9040 and the Department of
Biological Sciences, Columbia University, New York, New York 10027
,
-imino)triphosphate and adenosine
5'-3-O-(thio)triphosphate were poor analogues of ATP in terms of their ability to promote dimerization. Moreover, inclusion of MgCl2, substitution of KCl for NaCl, or
alterations in the polarity of the side chain at the catalytic base all
weakened the ATP-dependent dimer, suggesting that
electrostatic interactions are critical for the association reaction.
Thus, upon hydrolysis of bound ATP and the release of product, both
electrostatic and conformational changes drive the cassettes apart,
providing a second opportunity to couple free energy changes to the
transport reaction.
*
This work was supported by Robert Welch Foundation Grant
I-1284 and National Institutes of Health Grant DK49835 (to
P. J. T.).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.
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