Access the full text.
Sign up today, get DeepDyve free for 14 days.
A. Athanasiadis, D. Plácido, S. Maas, B. Brown, K. Lowenhaupt, Alexander Rich (2018)
The Crystal Structure of the Zβ Domain of the RNA-editing Enzyme ADAR1 Reveals Distinct Conserved Surfaces Among Z-domainsThe Excitement of Discovery: Selected Papers of Alexander Rich
Woonghee Lee, M. Tonelli, J. Markley (2014)
NMRFAM-SPARKY: enhanced software for biomolecular NMR spectroscopyBioinformatics, 31
W. Vranken, W. Boucher, T. Stevens, R. Fogh, A. Pajon, M. Llinás, E. Ulrich, J. Markley, J. Ionides, E. Laue (2005)
The CCPN data model for NMR spectroscopy: Development of a software pipelineProteins: Structure, 59
M. Cai, Ying Huang, Renbin Yang, R. Craigie, G. Clore (2016)
A simple and robust protocol for high-yield expression of perdeuterated proteins in Escherichia coli grown in shaker flasksJournal of Biomolecular NMR, 66
W. Fairbrother, IH A.G.Palmer, J. Skelton (1997)
Protein NMR Spectroscopy. Principles and PracticeZeitschrift für Physikalische Chemie, 202
M. Schade, C. Turner, K. Lowenhaupt, A. Rich, A. Herbert (1999)
Structure–function analysis of the Z‐DNA‐binding domain Zα of dsRNA adenosine deaminase type I reveals similarity to the (α + β) family of helix–turn–helix proteinsThe EMBO Journal, 18
F. Delaglio, S. Grzesiek, G. Vuister, G. Zhu, John Pfeifer, A. Bax (1995)
NMRPipe: A multidimensional spectral processing system based on UNIX pipesJournal of Biomolecular NMR, 6
Mary O’Connell, S. Krause, M. Higuchi, J. Hsuan, N. Totty, A. Jenny, W. Keller (1995)
Cloning of cDNAs encoding mammalian double-stranded RNA-specific adenosine deaminaseMolecular and Cellular Biology, 15
G. Ellis (2012)
The z -Domain
Mary O’Connell, W. Keller (1994)
Purification and properties of double-stranded RNA-specific adenosine deaminase from calf thymus.Proceedings of the National Academy of Sciences of the United States of America, 91 22
Thomas Schwartz, M. Rould, K. Lowenhaupt, A. Herbert, Alexander Rich (1999)
Crystal structure of the Zalpha domain of the human editing enzyme ADAR1 bound to left-handed Z-DNA.Science, 284 5421
J. Patterson, C. Samuel (1995)
Expression and regulation by interferon of a double-stranded-RNA-specific adenosine deaminase from human cells: evidence for two forms of the deaminaseMolecular and Cellular Biology, 15
Hachung Chung, J. Calis, Xianfang Wu, Tony Sun, Yingpu Yu, Stephanie Sarbanes, V. Thi, Abigail Shilvock, Hans-Heinrich Hoffmann, Brad Rosenberg, C. Rice (2018)
Human ADAR1 Prevents Endogenous RNA from Triggering Translational ShutdownCell, 172
B. Brown, K. Lowenhaupt, C. Wilbert, E. Hanlon, A. Rich (2000)
The zalpha domain of the editing enzyme dsRNA adenosine deaminase binds left-handed Z-RNA as well as Z-DNA.Proceedings of the National Academy of Sciences of the United States of America, 97 25
(2016)
2016) A simple and robust protocol
T. Schwartz, K. Lowenhaupt, Yang-Gyun Kim, Liyun Li, B. Brown, A. Herbert, A. Rich (1999)
Proteolytic Dissection of Zab, the Z-DNA-binding Domain of Human ADAR1*The Journal of Biological Chemistry, 274
B. Bass, H. Weintraub (1988)
An unwinding activity that covalently modifies its double-stranded RNA substrateCell, 55
C. George, Charles Samuel (1999)
Human RNA-specific adenosine deaminase ADAR1 transcripts possess alternative exon 1 structures that initiate from different promoters, one constitutively active and the other interferon inducible.Proceedings of the National Academy of Sciences of the United States of America, 96 8
J. Marsh, Vinay Singh, Z. Jia, J. Forman-Kay (2006)
Sensitivity of secondary structure propensities to sequence differences between α‐ and γ‐synuclein: Implications for fibrillationProtein Science, 15
A. Athanasiadis (2012)
Zalpha-domains: at the intersection between RNA editing and innate immunity.Seminars in cell & developmental biology, 23 3
M. Williamson (2013)
Using chemical shift perturbation to characterise ligand binding.Progress in nuclear magnetic resonance spectroscopy, 73
D. Plácido, B. Brown, K. Lowenhaupt, A. Rich, A. Athanasiadis (2007)
A Left-Handed RNA Double Helix Bound by the Zα Domain of the RNA-Editing Enzyme ADAR1Structure, 15
P. Montaville, N. Coudevylle, A. Radhakrishnan, A. Leonov, M. Zweckstetter, S. Becker
The PIP 2 binding mode of the C 2 domains of rabphilin-3 A
H. Kruse, Klaudia Mráziková, Luigi D’Ascenzo, J. Šponer, P. Auffinger (2020)
Short but weak! The Z-DNA lone-pair…π conundrum challenges standard carbon van der Waals radii.Angewandte Chemie
R. Wagner, J. Smith, B. Cooperman, K. Nishikura (1989)
A double-stranded RNA unwinding activity introduces structural alterations by means of adenosine to inosine conversions in mammalian cells and Xenopus eggs.Proceedings of the National Academy of Sciences of the United States of America, 86 8
A. Athanasiadis, D. Plácido, S. Maas, B. Brown, K. Lowenhaupt, A. Rich (2005)
The crystal structure of the Zbeta domain of the RNA-editing enzyme ADAR1 reveals distinct conserved surfaces among Z-domains.Journal of molecular biology, 351 3
Markus Schade, Christopher Turner, Ronald Kühne, P. Schmieder, K. Lowenhaupt, A. Herbert, Alexander Rich, Hartmut Oschkinat (1999)
The solution structure of the Zalpha domain of the human RNA editing enzyme ADAR1 reveals a prepositioned binding surface for Z-DNA.Proceedings of the National Academy of Sciences of the United States of America, 96 22
K. Nishikura (2015)
A-to-I editing of coding and non-coding RNAs by ADARsNature Reviews Molecular Cell Biology, 17
S. Hyberts, A. Milbradt, Andreas Wagner, H. Arthanari, G. Wagner (2012)
Application of iterative soft thresholding for fast reconstruction of NMR data non-uniformly sampled with multidimensional Poisson Gap schedulingJournal of Biomolecular NMR, 52
P. Montaville, N. Coudevylle, A. Radhakrishnan, A. Leonov, M. Zweckstetter, S. Becker (2008)
The PIP2 binding mode of the C2 domains of rabphilin‐3AProtein Science, 17
Alan Herbert, Markus Schade, K. Lowenhaupt, J. Alfken, Thomas Schwartz, L. Shlyakhtenko, Yuri Lyubchenko, Alexander Rich (1998)
The Zalpha domain from human ADAR1 binds to the Z-DNA conformer of many different sequences.Nucleic acids research, 26 15
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.
Biomolecular NMR Assignments – Springer Journals
Published: Oct 1, 2021
Keywords: ADAR1; Editing; Z-RNA; Protein structure and dynamics; Protein domains; Backbone chemical shift assignment
Read and print from thousands of top scholarly journals.
Already have an account? Log in
Bookmark this article. You can see your Bookmarks on your DeepDyve Library.
To save an article, log in first, or sign up for a DeepDyve account if you don’t already have one.
Copy and paste the desired citation format or use the link below to download a file formatted for EndNote
Access the full text.
Sign up today, get DeepDyve free for 14 days.
All DeepDyve websites use cookies to improve your online experience. They were placed on your computer when you launched this website. You can change your cookie settings through your browser.