Get 20M+ Full-Text Papers For Less Than $1.50/day. Start a 14-Day Trial for You or Your Team.

Learn More →

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

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 (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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biomolecular NMR Assignments Springer Journals

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

Loading next page...
 
/lp/springer-journals/solution-nmr-backbone-assignments-of-the-n-terminal-z-linker-z-segment-7rcMUxSGkq

References (31)

Publisher
Springer Journals
Copyright
Copyright © The Author(s), under exclusive licence to Springer Nature B.V. 2021
ISSN
1874-2718
eISSN
1874-270X
DOI
10.1007/s12104-021-10017-8
Publisher site
See Article on Publisher Site

Abstract

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.

Journal

Biomolecular NMR AssignmentsSpringer Journals

Published: Oct 1, 2021

Keywords: ADAR1; Editing; Z-RNA; Protein structure and dynamics; Protein domains; Backbone chemical shift assignment

There are no references for this article.