ATP Binding and Hydrolysis Properties of ABCB10 and Their Regulation by Glutathione
作者： Wei Qiu , Marc Liesa , Elizabeth P. Carpenter , Orian S. Shirihai
DOI: 10.1371/JOURNAL.PONE.0129772
关键词: Chemistry 、 Chemiosmosis 、 Oxidative phosphorylation 、 Mitochondrion 、 Adenosine triphosphate 、 ATP-binding cassette transporter 、 ATP hydrolysis 、 Walker motifs 、 ATP synthase alpha/beta subunits 、 Biochemistry
摘要: ABCB10 (ATP binding cassette sub-family B10) is a mitochondrial inner-membrane ABC transporter. has been shown to protect the heart from impact of ROS during ischemia-reperfusion and allow for proper hemoglobin synthesis erythroid development. transporters are proteins that increase ATP hydrolysis activity in presence transported substrate. However, molecular entities by its regulatory mechanisms currently unknown. Here we characterized properties using 8-azido-ATP photolabeling technique. This technique can identify potential regulators, substrates amino-acidic residues required hydrolysis. We confirmed Gly497 Lys498 Walker A motif, Glu624 B motif Gly602 C-Loop activity, as their mutation changed 8-Azido-ATP photo-labeling. In addition, show entity heme precursor delta-aminolevulinic acid (dALA) does not alter contrast, oxidized glutathione (GSSG) stimulates without affecting binding, whereas reduced (GSH) inhibits Indeed, detectABCB10 glutathionylation Cys547 it one exposed cysteine within structure. all, characterize essential ATPase provide evidence supports exclusion dALA substrate directly ABCB10. Last, first mechanism which oxidative status, through GSH/GSSG, regulate
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