Conformational exchange of the Zα domain of human RNA editing enzyme ADAR1 studied by NMR spectroscopy
| Autor: | Hye-Bin Ahn, Ae-Ree Lee, Youyeon Go, Joon-Hwa Lee, Kwang-Im Oh, Byeong-Seon Kim |
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| Rok vydání: | 2021 |
| Předmět: |
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Molecular Adenosine Deaminase Protein Conformation Population Biophysics Biochemistry Hydrophobic effect chemistry.chemical_compound Protein Domains Humans Protein–DNA interaction education Molecular Biology Nuclear Magnetic Resonance Biomolecular education.field_of_study Chemistry Protein dynamics RNA-Binding Proteins Cell Biology Nuclear magnetic resonance spectroscopy Kinetics RNA editing Z-DNA Binding Protein RNA Editing Hydrophobic and Hydrophilic Interactions DNA |
| Zdroj: | Biochemical and biophysical research communications. 580 |
| ISSN: | 1090-2104 |
| Popis: | Z-DNA binding proteins (ZBPs) play important roles in RNA editing, innate immune responses, and viral infections. Numerous studies have implicated a role for conformational motions during ZBPs binding upon DNA, but the quantitative intrinsic conformational exchanges of ZBP have not been elucidated. To understand the correlation between the biological function and dynamic feature of the Zα domains of human ADAR1 (hZαADAR1), we have performed the 15N backbone amide Carr-Purcell-Meiboom-Gill (CPMG) relaxation dispersion experiments on the free hZαADAR1 at two different magnetic fields at 35 °C. The robust inter-dependence of parameters in the global fitting process using multi-magnetic field CPMG profiles allows us characterizing the dynamic properties of conformational changes in hZαADAR1. This study found that free hZαADAR1 exhibited the conformational exchange with a kex of 5784 s−1 between the states “A” (89% population) and “B” (11% population). The different hydrophobic interactions among helices α1, α2, and α3 between these two states might correlate with efficient Z-DNA binding achieved by the hydrogen bonding interactions between its side-chains and the phosphate backbone of Z-DNA. |
| Databáze: | OpenAIRE |
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