Histone fold

A histone fold is a structurally conserved motif found near the C-terminus in every core histone sequence in a histone octamer responsible for the binding of histones into heterodimers.

The histone fold averages about 70 amino acids and consists of three alpha helices connected by two short, unstructured loops.[1] When not in the presence of DNA, the core histones assemble into head-to-tail intermediates (H3 and H4 first assemble into heterodimers then fuse two heterodimers to form a tetramer, while H2A and H2B form heterodimers[2]) via extensive hydrophobic interactions between each histone fold domain in a "handshake motif".[3]

References

  1. ↑ Alva, V., Ammelburg, M., Soding, J. & Lupas, A.N. (2007). On the origin of the histone fold. BioMed Central Structural Biology. 7(17). doi: 10.1186/1472-6807-7-17
  2. ↑ Watson et al. (2007). Molecular biology of the gene. Benjamin Cummings. pp. 224
  3. ↑ Arrents, G. & Mourdrianakis, E.N. (1995). The histone fold: A ubiquitous architectural motif utilized in DNA compaction and protein dimerization. PNAS. 92, 11170-11174. Retrieved from http://www.pnas.org/content/92/24/11170.full.pdf


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