Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

An ADAR that edits transcripts encoding ion channel subunits functions as a dimer.

Angela Gallo1, Liam P Keegan, Gillian M Ring

  • 1MRC Human Genetics Unit, Western General Hospital, Crewe Road, Edinburgh EH4 2XU, UK.

The EMBO Journal
|July 4, 2003
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Pediatric High-Grade Gliomas and Cancer Predisposition Syndromes: A Retrospective Study.

HGG advances·2026
Same author

Reconfigured immunity in Adar heterozygous and Adar Mavs Eif2ak2 (PKR) triple mutant mice.

RNA (New York, N.Y.)·2026
Same author

ADAR1 and ADAR2 associate with the RNA exosome and modulate RNA stability.

Nucleic acids research·2026
Same author

ADAR2 induces the differentiation of osteosarcoma cells by editing activity on IGFBP7: new implications for therapy.

Bone research·2026
Same author

Editing-independent effects of <i>Drosophila</i> Adar on heterochromatin silencing.

RNA (New York, N.Y.)·2026
Same author

Microgliosis and aberrant interferon response in Adar Mavs brain are rescued by PKR removal.

Brain : a journal of neurology·2025

Drosophila adenosine deaminase acting on RNA (ADAR) requires dimerization on double-stranded RNA for editing activity. Dimer formation, involving the N-terminus and dsRNA-binding domain 1, is crucial for this essential biological process.

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • Adenosine deaminase acting on RNA (ADAR) enzymes are critical for RNA editing.
  • The mechanisms regulating ADAR activity, particularly its dimerization, are not fully understood.

Purpose of the Study:

  • To investigate the molecular requirements for Drosophila ADAR dimerization.
  • To determine the relationship between ADAR dimerization, RNA binding, and enzymatic activity.

Main Methods:

  • Site-directed mutagenesis to identify key domains for dimerization.
  • Glycerol gradient centrifugation to analyze protein complex formation.
  • In vitro RNA editing assays to assess enzyme activity.

Main Results:

Related Experiment Videos

  • Drosophila ADAR dimerization on double-stranded RNA is essential for editing.
  • The N-terminus and dsRNA-binding domain 1 (dsRBD1) are necessary for dimerization.
  • Mutations in dsRBD1 abolish both RNA binding and dimerization.
  • ADAR can bind RNA as a monomer but requires dimerization for editing activity.
  • Heterodimerization of different ADAR isoforms affects editing efficiency.

Conclusions:

  • ADAR functions as an active dimer, not a monomer.
  • Dimerization is a critical regulatory step for ADAR-mediated RNA editing.
  • Understanding ADAR dimerization provides insights into RNA editing mechanisms and potential therapeutic targets.