NDLI: ATP and AMP Mutually Influence Their Interaction with the ATP-binding Cassette (ABC) Adenylate Kinase Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) at Separate Binding $Sites^{*}$ $^{}$

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ATP and AMP Mutually Influence Their Interaction with the ATP-binding Cassette (ABC) Adenylate Kinase Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) at Separate Binding $Sites^{*}$ $^{}$

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ATP and AMP Mutually Influence Their Interaction with the ATP-binding Cassette (ABC) Adenylate Kinase Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) at Separate Binding $Sites^{*}$ $^{}$

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Elcock, Adrian H. Dong, Qian Welsh, Michael J. Ver Heul, Amanda R. Randak, Christoph O.
Description	Author Affiliation: Randak CO ( From the Departments of Pediatrics.)
Abstract	Cystic fibrosis transmembrane conductance regulator (CFTR) is an anion channel in the ATP-binding cassette (ABC) transporter protein family. In the presence of ATP and physiologically relevant concentrations of AMP, CFTR exhibits adenylate kinase activity (ATP + AMP ⇆ 2 ADP). Previous studies suggested that the interaction of nucleotide triphosphate with CFTR at ATP-binding site 2 is required for this activity. Two other ABC proteins, Rad50 and a structural maintenance of chromosome protein, also have adenylate kinase activity. All three ABC adenylate kinases bind and hydrolyze ATP in the absence of other nucleotides. However, little is known about how an ABC adenylate kinase interacts with ATP and AMP when both are present. Based on data from non-ABC adenylate kinases, we hypothesized that ATP and AMP mutually influence their interaction with CFTR at separate binding sites. We further hypothesized that only one of the two CFTR ATP-binding sites is involved in the adenylate kinase reaction. We found that 8-azidoadenosine 5′-triphosphate $(8-N_{3}-ATP)$ and 8-azidoadenosine 5′-monophosphate $(8-N_{3}-AMP)$ photolabeled separate sites in CFTR. Labeling of the AMP-binding site with $8-N_{3}-AMP$ required the presence of ATP. Conversely, AMP enhanced photolabeling with $8-N_{3}-ATP$ at ATP-binding site 2. The adenylate kinase active center probe $P^{1},P^{5}-di(adenosine-5′)$ pentaphosphate interacted simultaneously with an AMP-binding site and ATP-binding site 2. These results show that ATP and AMP interact with separate binding sites but mutually influence their interaction with the ABC adenylate kinase CFTR. They further indicate that the active center of the adenylate kinase comprises ATP-binding site 2.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	38
Volume Number	288
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2013-09-20
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Adenosine Monophosphate Chemistry Adenosine Triphosphate Adenylate Kinase Cystic Fibrosis Transmembrane Conductance Regulator Genetics Metabolism Analogs & Derivatives Binding Sites HeLa Cells Protein Structure, Tertiary Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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