Related Experiment Video
Updated: Jun 15, 2026

Single-Molecule Imaging of EWS-FLI1 Condensates Assembling on DNA
Published on: September 8, 2021
The T/E1A-binding domain of the retinoblastoma product can interact selectively with a sequence-specific DNA-binding
T Chittenden1, D M Livingston, W G Kaelin
1Dana-Farber Cancer Institute, Boston, Massachusetts 02115.
Abstract:
A DNA-binding site selection and enrichment procedure revealed a sequence-specific DNA-binding activity selectively associated with glutathione S-transferase-retinoblastoma protein chimeras (GST-RB) that had been incubated with a human cell extract. Appropriate mutant forms of GST-RB, incubated in equivalent extracts, did not associate with this specific DNA-binding activity, and a peptide replica of the HPV E7 RB-binding segment selectively inhibited the association of GST-RB with the sequence-specific DNA-binding protein(s). Sequence analysis of oligonucleotides with high affinity for GST-RB complexes, as well as the results of competition binding studies, strongly suggest that RB can associate specifically with the transcription factor E2F or with a protein having closely related DNA-binding properties.
Related Concept Videos
Conservative Site-specific Recombination and Phase Variation
The recognition sites for Cre recombinase called LoxP...
Tumor Immunotherapy

