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Updated: Jul 28, 2026

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Genome-wide Analysis using ChIP to Identify Isoform-specific Gene Targets
Published on: July 7, 2010
Mutational analysis of the J recombination signal sequence binding protein (RBP-J)/Epstein-Barr virus nuclear antigen
K P Fuchs1, G Bommer, E Dumont
1Institut für Klinische Molekularbiologie und Tumorgenetik, GSF Forschungszentrum für Umwelt und Gesundheit, München, Germany.
European Journal of Biochemistry
|September 5, 2001
Summary
Epstein-Barr virus nuclear antigen 2 (EBNA2) and Notch proteins interact with RBP-J. Mutational analysis identified specific RBP-J amino acids crucial for these interactions, potentially targeting EBV-related diseases.
Area of Science:
- Molecular Biology
- Virology
- Cell Biology
Background:
- Epstein-Barr virus nuclear antigen 2 (EBNA2) is vital for B-cell immortalization by Epstein-Barr virus (EBV).
- Notch proteins regulate cell fate and are implicated in lymphomagenesis.
- Both EBNA2 and Notch proteins interact with the DNA-binding protein RBP-J to access target gene promoters.
Purpose of the Study:
- To identify specific regions within RBP-J critical for its interaction with either EBNA2 or Notch.
- To understand the molecular basis of EBNA2-RBP-J and Notch-RBP-J protein-protein interactions.
Main Methods:
- Performed a mutational analysis of RBP-J.
- Screened a library of RBP-J mutants using a reverse two-hybrid system to identify binding-deficient alleles for EBNA2 or Notch.
Main Results:
- Identified a limited set of distinct amino acid positions in RBP-J essential for selective binding to either EBNA2 or Notch.
- Sequence analysis of mutants revealed specific residues mediating these differential interactions.
Conclusions:
- The EBNA2/RBP-J protein-protein interaction is a potential therapeutic target for EBV-related diseases.
- Understanding these specific interactions provides insights into viral pathogenesis and cellular signaling pathways.
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