Molecular characterization of human double-stranded RNA specific adenosine deaminases (ADARs)
Adenosine deaminases acting on RNA (ADARs) are enzymes that performs adenosine-to-inosine (A-to-I) editing via adenosine deamination. The RNA editing capacity of the proteins makes ADARs major players in the regulation of important gene products, modulation of immune responses, outcome of viral i...
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| Other Authors: | |
| Format: | Final Year Project (FYP) |
| Language: | English |
| Published: |
2016
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| Online Access: | http://hdl.handle.net/10356/67909 |
| _version_ | 1811696822352084992 |
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| author | Ong, Zi Xin |
| author2 | Luo Dahai |
| author_facet | Luo Dahai Ong, Zi Xin |
| author_sort | Ong, Zi Xin |
| collection | NTU |
| description | Adenosine deaminases acting on RNA (ADARs) are enzymes that performs adenosine-to-inosine
(A-to-I) editing via adenosine deamination. The RNA editing capacity of the proteins makes
ADARs major players in the regulation of important gene products, modulation of immune
responses, outcome of viral infections, oncogenesis, and even developmental processes.
Understanding the mechanism behind ADARs’ RNA substrate binding and catalysis would shed
light on mechanisms of diseases related to ADAR dysfunction. In this study, soluble
recombinant protein constructs of various ADAR1 and ADARB1 domains were generated.
Sequence and structural requirements of RNA substrates were explored using various short
dsRNA constructs. A spontaneous dissociation of ADAR1 dsRBD3 from the editase domain was
observed, suggesting the solubility and activity of the ADAR1 editase domain alone. In addition,
blunt-ended dsRNA as short as 10bp displayed good binding affinity to ADAR1 and ADARB1,
suggesting the usefulness of short dsRNA substrates in protein-RNA co-crystallization. The
results provide the basis to further study ADAR protein-RNA binding and catalysis. |
| first_indexed | 2024-10-01T07:45:28Z |
| format | Final Year Project (FYP) |
| id | ntu-10356/67909 |
| institution | Nanyang Technological University |
| language | English |
| last_indexed | 2024-10-01T07:45:28Z |
| publishDate | 2016 |
| record_format | dspace |
| spelling | ntu-10356/679092023-02-28T18:04:22Z Molecular characterization of human double-stranded RNA specific adenosine deaminases (ADARs) Ong, Zi Xin Luo Dahai School of Biological Sciences DRNTU::Science Adenosine deaminases acting on RNA (ADARs) are enzymes that performs adenosine-to-inosine (A-to-I) editing via adenosine deamination. The RNA editing capacity of the proteins makes ADARs major players in the regulation of important gene products, modulation of immune responses, outcome of viral infections, oncogenesis, and even developmental processes. Understanding the mechanism behind ADARs’ RNA substrate binding and catalysis would shed light on mechanisms of diseases related to ADAR dysfunction. In this study, soluble recombinant protein constructs of various ADAR1 and ADARB1 domains were generated. Sequence and structural requirements of RNA substrates were explored using various short dsRNA constructs. A spontaneous dissociation of ADAR1 dsRBD3 from the editase domain was observed, suggesting the solubility and activity of the ADAR1 editase domain alone. In addition, blunt-ended dsRNA as short as 10bp displayed good binding affinity to ADAR1 and ADARB1, suggesting the usefulness of short dsRNA substrates in protein-RNA co-crystallization. The results provide the basis to further study ADAR protein-RNA binding and catalysis. Bachelor of Science in Biological Sciences 2016-05-23T06:58:23Z 2016-05-23T06:58:23Z 2016 Final Year Project (FYP) http://hdl.handle.net/10356/67909 en Nanyang Technological University 45 p. application/pdf |
| spellingShingle | DRNTU::Science Ong, Zi Xin Molecular characterization of human double-stranded RNA specific adenosine deaminases (ADARs) |
| title | Molecular characterization of human double-stranded RNA specific adenosine deaminases (ADARs) |
| title_full | Molecular characterization of human double-stranded RNA specific adenosine deaminases (ADARs) |
| title_fullStr | Molecular characterization of human double-stranded RNA specific adenosine deaminases (ADARs) |
| title_full_unstemmed | Molecular characterization of human double-stranded RNA specific adenosine deaminases (ADARs) |
| title_short | Molecular characterization of human double-stranded RNA specific adenosine deaminases (ADARs) |
| title_sort | molecular characterization of human double stranded rna specific adenosine deaminases adars |
| topic | DRNTU::Science |
| url | http://hdl.handle.net/10356/67909 |
| work_keys_str_mv | AT ongzixin molecularcharacterizationofhumandoublestrandedrnaspecificadenosinedeaminasesadars |