Related Experiment Video
Updated: Jan 12, 2026
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Deciphering Molecular Mechanism of Histone Assembly by DNA Curtain Technique
Published on: March 9, 2022
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Large Extent of Convergent Evolution Towards the Double Histone Fold Revealed by Targeted Sequence and Structure
Toshiko Miyake1, Anna Ranaudo2, Elena Sacco3
1Department of Pharmaceutical and Pharmacological Sciences, University of Padova, Padova, Italy.
Proteins
|November 7, 2025
Summary
The double histone fold, previously thought rare, is widespread in eukaryotes. This finding opens new avenues in epigenetics and DNA-binding protein design.
Area of Science:
- Molecular Biology
- Structural Biology
- Genomics
Background:
- Histone proteins are essential for chromatin packaging in eukaryotes.
- Nucleosomal cores, fundamental units of DNA packaging, are formed by histone dimers.
- The double histone fold, a structure where two histone folds form a pseudodimer, was considered uncommon.
Purpose of the Study:
- To investigate the prevalence of the double histone fold in eukaryotes.
- To analyze the structural and sequence characteristics of the double histone fold.
- To explore the implications of the double histone fold's widespread nature.
Main Methods:
- Protein structure analysis.
- Sequence analysis across eukaryotic genomes.
Main Results:
- The double histone fold is not uncommon but widespread across eukaryotic organisms.
- Structural and sequence data support the broad occurrence of this fold.
Conclusions:
- The double histone fold is a conserved and prevalent structural motif in eukaryotes.
- This finding has significant implications for understanding epigenetics and designing novel DNA-binding proteins.
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