Interactions between Metal-binding Domains Modulate Intracellular Targeting of Cu(I)-ATPase ATP7B, as Revealed by Nanobody Binding
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چکیده
منابع مشابه
Lis1 Acts as a “Clutch” between the ATPase and Microtubule-Binding Domains of the Dynein Motor
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Rachel Linz,* Natalie L. Barnes,* Adriana M. Zimnicka, Jack H. Kaplan, Betty Eipper, and Svetlana Lutsenko Department of Biochemistry and Molecular Biology, Oregon Health and Science University, Portland, Oregon; Department of Biochemistry and Molecular Genetics, University of Illinois, Chicago, Illinois; and Department of Neuroscience, University of Connecticut Health Center, Farmington, Conne...
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The putative copper binding domain from the copper-transporting ATPase implicated in Wilson disease (ATP7B) has been expressed and purified as a fusion to glutathione S-transferase. Immobilized metal ion affinity chromatography revealed that the fusion protein is able to bind to columns charged with different transition metals with varying affinities as follows: Cu(II)>>Zn(II)>Ni(II)>Co(II). Th...
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Chromatin remodellers are ATP-dependent motor proteins that physically reposition and reorganize nucleosomes. Chd1 and Iswi-type remodellers possess a DNA-binding domain (DBD) needed for efficient nucleosome mobilization; however, it has not been clear how this domain physically contributes to remodelling. Here we show that the Chd1 DBD promotes nucleosome sliding simply by tethering the remode...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2014
ISSN: 0021-9258
DOI: 10.1074/jbc.m114.580845