Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 288, Issue 29, Pages 20785-20796Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M113.477976
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Funding
- National Institutes of Health [R01GM79629, 3R01GM079629-03S1]
- Cancer Prevention & Research Institute of Texas Grant [RP101073]
- American Heart Association Predoctoral Fellowship [11PRE7360046]
- Lubbock Chapter of the Achievement Rewards for College Scientists Foundation
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In ATP-binding cassette proteins, the two nucleotide-binding domains (NBDs) work as dimers to bind and hydrolyze ATP, but the molecular mechanism of nucleotide hydrolysis is controversial. It is still unresolved whether hydrolysis leads to dissociation of the ATP-induced dimers or partial opening of the dimers such that the NBDs remain in contact during the hydrolysis cycle. We studied the bacterial lipid flippase MsbA by luminescence resonance energy transfer (LRET). The LRET signal between optical probes reacted with single-cysteine mutants was employed to follow NBD association/dissociation in real time. The intermonomer distances calculated from LRET data indicate that the NBDs separate completely following ATP hydrolysis, even in the presence of mM MgATP, and that the dissociation occurs following each hydrolysis cycle. The results support association/dissociation, as opposed to constant contact models, for the mode of operation of ATP-binding cassette proteins.
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