Related Experiment Video
Updated: Jul 18, 2026

06:48
CD Spectroscopy to Study DNA-Protein Interactions
Published on: February 10, 2022
Inverted factor access and slow reversion characterize SWI/SNF-altered nucleosome dimers
Natalia P Ulyanova1, Gavin R Schnitzler
1Department of Biochemistry, Tufts University School of Medicine, Boston, Massachusetts 02111, USA.
The Journal of Biological Chemistry
|November 24, 2006
Summary
Human SWI/SNF (hSWI/SNF) remodeling complexes alter nucleosome structures, forming dimers and altosomes. These altered forms exhibit unique DNA accessibility profiles and influence transcription factor binding, impacting gene regulation.
Area of Science:
- Chromatin biology
- Molecular genetics
- Biochemistry
Background:
- The human SWI/SNF (hSWI/SNF) complex is crucial for gene regulation through ATP-dependent chromatin remodeling.
- Previous studies demonstrated hSWI/SNF's ability to generate structurally altered nucleosome dimers from mononucleosomes.
- Recent findings indicated hSWI/SNF also produces structurally altered dinucleosomes, termed altosomes, from polynucleosomal templates.
Purpose of the Study:
- To propose a unified model for hSWI/SNF-generated nucleosome products (dimers and altosomes).
- To investigate the DNA accessibility within these altered nucleosome structures for transcription factors.
- To explore the reciprocal influence between hSWI/SNF products and transcription factor binding.
Main Methods:
- Biophysical characterization of nucleosome structures and dynamics.
- Analysis of DNA accessibility using biochemical assays.
- Investigating transcription factor interactions with altered nucleosomes.
Main Results:
- Dinucleosomes (altosomes) and dimers generated by hSWI/SNF revert to normal nucleosomes at comparable rates.
- Altered dimers can be cleaved into particles resembling mononucleosomes.
- DNA accessibility in altered dimers is highest in the middle and lowest at the ends, contrasting with normal mononucleosomes.
- Transcription factor binding affects the equilibrium between normal nucleosomes and hSWI/SNF-generated dimers.
Conclusions:
- A single model can explain the formation and properties of both hSWI/SNF-altered dimers and altosomes.
- The distinct DNA accessibility profile of altered dimers has significant implications for transcription factor access.
- Transcription factors and hSWI/SNF products engage in a dynamic interplay that influences chromatin structure and gene expression.
Related Concept Videos
Nucleosome Remodeling
Nucleosomes are the basic units of chromatin compaction. Each nucleosome consists of the DNA bound tightly around a histone core, which makes the DNA inaccessible to DNA binding proteins such as DNA polymerase and RNA polymerase. Hence, the fundamental problem is to ensure access to DNA when appropriate, despite the compact and protective chromatin structure.
Nucleosome remodeling complex
Eukaryotic cells have specialized enzymes called ATP-dependent nucleosome remodeling enzymes. These enzymes...
Nucleosome remodeling complex
Eukaryotic cells have specialized enzymes called ATP-dependent nucleosome remodeling enzymes. These enzymes...
Restarting Stalled Replication Forks
DNA replication is initiated at sites containing predefined DNA sequences known as origins of replication. DNA is unwound at these sites by the minichromosome maintenance (MCM) helicase and other factors such as Cdc45 and the associated GINS complex.The unwound single strands are protected by replication protein A (RPA) until DNA polymerase starts synthesizing DNA at the 5’ end of the strand in the same direction as the replication fork. To prevent the replication fork from falling apart, a...
Conservative Site-specific Recombination and Phase Variation
Because the DNA segments are cut and reorganized in a direction-specific manner, site-specific recombination has emerged as an efficient genetic engineering technique. Flippase and Cyclization recombinases or Flp and Cre, respectively, are two members of the tyrosine recombinase family derived from bacteriophages, that are used to mediate site-specific DNA insertions, deletions, and targeted expression of proteins in mammalian cell lines.
The recognition sites for Cre recombinase called LoxP...
The recognition sites for Cre recombinase called LoxP...
Position-effect Variegation
In 1928, a German botanist Emil Heitz observed the moss nuclei with a DNA binding dye. He observed that while some chromatin regions decondense and spread out in the interphase nucleus, others do not. He termed them euchromatin and heterochromatin, respectively. He proposed that the heterochromatin regions reflect a functionally inactive state of the genome. It was later confirmed that heterochromatin is transcriptionally repressed, and euchromatin is transcriptionally active chromatin.
The Nucleosome Core Particle
Nucleosomes are the DNA-histone complex, where the DNA strand is wound around the histone core. The histone core is an octamer containing two copies of H2A, H2B, H3, and H4 histone proteins.
The paradox
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their main responsibility is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. While on the other hand, they must allow polymerase enzymes to access DNA...
The paradox
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their main responsibility is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. While on the other hand, they must allow polymerase enzymes to access DNA...

