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J. Biol. Chem., Vol. 278, Issue 29, 26862-26869, July 18, 2003
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From the Institute of Biochemistry, Biocenter, J. W. Goethe-University, Marie-Curie-Str. 9, D-60439 Frankfurt a.M., Germany
The ABC transporter Mdl1p, a structural and functional homologue of the
transporter associated with antigen processing (TAP) plays an important role
in intracellular peptide transport from the mitochondrial matrix of
Saccharomyces cerevisiae. To characterize the ATP hydrolysis cycle of
Mdl1p, the nucleotide-binding domain (NBD) was overexpressed in
Escherichia coli and purified to homogeneity. The isolated NBD was
active in ATP binding and hydrolysis with a turnover of 25 ATP per minute and
a Km of 0.6 mM and did not show
cooperativity in ATPase activity. However, the ATPase activity was
non-linearly dependent on protein concentration (Hill coefficient of 1.7),
indicating that the functional state is a dimer. Dimeric catalytic transition
states could be trapped either by incubation with orthovanadate or beryllium
fluoride, or by mutagenesis of the NBD. The nucleotide composition of trapped
intermediate states was determined using [
-32P]ATP and
[
-32P]ATP. Three different dimeric intermediate states were
isolated, containing either two ATPs, one ATP and one ADP, or two ADPs. Based
on these experiments, it was shown that: (i) ATP binding to two NBDs induces
dimerization, (ii) in all isolated dimeric states, two nucleotides are
present, (iii) phosphate can dissociate from the dimer, (iv) both nucleotides
are hydrolyzed, and (v) hydrolysis occurs in a sequential mode. Based on these
data, we propose a processive-clamp model for the catalytic cycle in which
association and dissociation of the NBDs depends on the status of bound
nucleotides.
Received for publication, February 4, 2003 , and in revised form, May 3, 2003.
* The work was supported by the Deutsche Forschungsgemeinschaft. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
Supported by a TALENT fellowship from the Netherlands Organization for
Scientific Research (NWO).
To whom correspondence should be addressed. Tel.: 49-69-798-29475; Fax:
49-69-798-29495; E-mail:
tampe{at}em.uni-frankfurt.de.
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