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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Veröffentlicht in:	Biomolecular NMR assignments Jg. 15; H. 2; S. 273 - 279
Hauptverfasser:	Nichols, Parker J., Henen, Morkos A., Vicens, Quentin, Vögeli, Beat
Format:	Journal Article
Sprache:	Englisch
Veröffentlicht:	Dordrecht Springer Netherlands 01.10.2021 Springer Nature B.V
Schlagworte:	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-Zugang:	Volltext
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Zusammenfassung:	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.
Bibliographie:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23
ISSN:	1874-2718 1874-270X 1874-270X
DOI:	10.1007/s12104-021-10017-8