Please use this identifier to cite or link to this item:
Full metadata record
DC FieldValueLanguage
dc.contributor.authorOng, Zi Xin-
dc.description.abstractAdenosine 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.en_US
dc.format.extent45 p.en_US
dc.rightsNanyang Technological University-
dc.titleMolecular characterization of human double-stranded RNA specific adenosine deaminases (ADARs)en_US
dc.typeFinal Year Project (FYP)en_US
dc.contributor.supervisorLuo Dahaien_US
dc.contributor.schoolSchool of Biological Sciencesen_US
dc.description.degreeBachelor of Science in Biological Sciencesen_US
item.fulltextWith Fulltext-
Appears in Collections:SBS Student Reports (FYP/IA/PA/PI)
Files in This Item:
File Description SizeFormat 
  Restricted Access
3.47 MBAdobe PDFView/Open

Page view(s)

Updated on Jun 17, 2021

Download(s) 50

Updated on Jun 17, 2021

Google ScholarTM


Items in DR-NTU are protected by copyright, with all rights reserved, unless otherwise indicated.