The Origin of the Histone Fold
Author Information
Author(s): Alva Vikram, Ammelburg Moritz, Söding Johannes, Lupas Andrei N
Primary Institution: Max-Planck-Institute for Developmental Biology
Hypothesis
Folded proteins evolved by combination of an ancestral set of peptides, the antecedent domain segments.
Conclusion
The helix-strand-helix motif common to these three folds supports the theory of an 'ancient peptide world' by showing how an ancestral fragment can give rise to three different folds.
Supporting Evidence
- The study found an evolutionary relationship between histone proteins and the helical part of the extended AAA+ ATPase domain.
- The results suggest that an ancestral helix-strand-helix motif gave rise to three different protein folds.
- This research presents the first example of a genetically fixed 3D domain swap leading to a new protein family.
Takeaway
Scientists studied how a specific protein structure called the histone fold evolved from simpler building blocks, showing that proteins can change and develop new shapes over time.
Methodology
Sequence and structure comparisons were used to investigate the evolutionary origin of the histone fold.
Digital Object Identifier (DOI)
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