ArticleProceedings of the National Academy of Sciences of the United States of America2011
Experimental evidence for the role of domain swapping in the evolution of the histone fold.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Insights into mechanisms and significance of domain swapping from emerging examples in the Mog1p/PsbP-like fold.Biochemical and biophysical research communications · 2025Review
- Designing monomeric IFNγ: The significance of domain-swapped dimer structure in IFNγ immune responses.The Journal of biological chemistry · 2024Article
- Dual-wield NTPases: A novel protein family mined from AlphaFold DB.Protein science : a publication of the Protein Society · 2024Article
- Experimental and theoretical study on converting myoglobin into a stable domain-swapped dimer by utilizing a tight hydrogen bond network at the hinge region.RSC advances · 2021Article
- Human FoxP Transcription Factors as Tractable Models of the Evolution and Functional Outcomes of Three-Dimensional Domain Swapping.International journal of molecular sciences · 2021Review
- A five-residue motif for the design of domain swapping in proteins.Nature communications · 2019Article
- Transient misfolding dominates multidomain protein folding.Nature communications · 2015Article
- An archaeal histone is required for transformation of Thermococcus kodakarensis.Journal of bacteriology · 2012Article
- Article
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The histone fold forms the fundamental endoskeleton of the protein core of the nucleosome and is also found in several transcription factors. We have investigated the evolutionary origins of this ubiquitous protein motif, which is found soluble exclusively as an antiparallel (handshake motif) dimer. We introduced a three amino acid insertion into the middle of a homodimeric archaeal histone fold motif. The engineered molecule was found to be a soluble and stable monomer with properties consistent with a four-helix-bundle protein. The experimental evidence presented here support the hypothesis that the handshake association motif characteristic of present-day histone dimers is the evolutionary product of domain swapping between two four-helix bundle domains, each of which derived from the tandem duplication of a primitive helix-strand-helix unit.
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