Solution NMR backbone assignments of the N-terminal Zα-linker-Zβ segment from Homo sapiens ADAR1p150

Adenosine-to-inosine (A-to-I) editing of a subset of RNAs in a eukaryotic cell is required in order to avoid triggering the innate immune system. Editing is carried out by ADAR1, which exists as short (p110) and long (p150) isoforms. ADAR1p150 is mostly cytoplasmic, possesses a Z-RNA binding domain...

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Published in:Biomolecular NMR assignments Vol. 15; no. 2; pp. 273 - 279
Main Authors: Nichols, Parker J., Henen, Morkos A., Vicens, Quentin, Vögeli, Beat
Format: Journal Article
Language:English
Published: Dordrecht Springer Netherlands 01.10.2021
Springer Nature B.V
Subjects:
Adenosine
Adenosine Deaminase - chemistry
Adenosine Deaminase - metabolism
Amino Acid Sequence
Biochemistry
Biological and Medical Physics
Biophysics
Humans
Immune response
Innate immunity
Isoforms
N-Terminus
NMR
Nuclear magnetic resonance
Nuclear Magnetic Resonance, Biomolecular
Physics
Physics and Astronomy
Polymer Sciences
Protein Domains
Protein structure
RNA-Binding Proteins - chemistry
RNA-Binding Proteins - metabolism
Secondary structure
Solutions
Editing
Protein domains
Z-RNA
Protein structure and dynamics
Backbone chemical shift assignment
ADAR1
ISSN:1874-2718, 1874-270X, 1874-270X
Online Access:Get full text
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Summary:Adenosine-to-inosine (A-to-I) editing of a subset of RNAs in a eukaryotic cell is required in order to avoid triggering the innate immune system. Editing is carried out by ADAR1, which exists as short (p110) and long (p150) isoforms. ADAR1p150 is mostly cytoplasmic, possesses a Z-RNA binding domain (Zα), and is only expressed during the innate immune response. A structurally homologous domain to Zα, the Zβ domain, is separated by a long linker from Zα on the N-terminus of ADAR1 but its function remains unknown. Zβ does not bind to RNA in isolation, yet the binding kinetics of the segment encompassing Zα, Zβ and the 95-residue linker between the two domains (Zα–Zβ) are markedly different compared to Zα alone. Here we present the solution NMR backbone assignment of Zα–Zβ from H. Sapiens ADAR1. The predicted secondary structure of Zα–Zβ based on chemical shifts is in agreement with previously determined structures of Zα and Zβ in isolation, and indicates that the linker is intrinsically disordered. Comparison of the chemical shifts between the individual Zα and Zβ domains to the full Zα–Zβ construct suggests that Zβ may interact with the linker, the function of which is currently unknown.
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ISSN:1874-2718
1874-270X
1874-270X
DOI:10.1007/s12104-021-10017-8