Double histone fold

Available protein structures:
PDB	IPR015207
AlphaFold	IPR015207;

Double histone fold
Double histone fold
Identifiers
Symbol	DHF
InterPro	IPR015207
PDB
Available protein structures:
PDB	IPR015207
AlphaFold	IPR015207;

The double histone fold is a tertiary fold usually (but not exclusively) found in proteins that bind DNAs, such as archaeal histones.^[1] This fold is composed of distinct alpha helical segments organized in pairs of triplets that fold intramolecularly to give place to a globular assembly structurally similar to a histone dimer.

Double histone fold proteins are relatively rare. The fold is quite versatile in that it can mediate various functions, either related or unrelated to chromatin organization. They can function as intramolecular modulator of enzyme activity, transcription factors, and proteins related to viral pathogenicity in addition to the traditional role.

History

The double histone fold was first described by Dr. Slesarev and coworkers in 2001.^[2] He and coworkers were the first to deduce the structure of Methanopyrus kandleri histone and characterized the structural motif within this protein which would later be called the double histone fold.^[3] It was subsequently found that very diverse proteins, such as viral proteins and eukaryotic multidomain proteins contain this same structurally conserved double histone fold motif.^[1]

References

1 2 Ranaudo A, Miyake T, Cosentino U, Greco C (May 2026). "The double histone fold: Structure, functional implications across the tree of life and relevance to protein design". Protein Science. 35 (5) e70573. doi:10.1002/pro.70573. PMC 13088155. PMID 41994963.
↑ Fahrner RL, Cascio D, Lake JA, Slesarev A (March 2001). "An ancestral nuclear protein assembly: crystal structure of the Methanopyrus kandleri histone". Protein Science. 10 (10): 2002–2007. doi:10.1110/ps.10901. PMC 2374223. PMID 11567091.
↑ Greco C, Sacco E, Vanoni M, De Gioia L (October 2005). "Identification and in silico analysis of a new group of double-histone fold-containing proteins". Journal of Molecular Modeling. 12 (1): 76–84. doi:10.1007/s00894-005-0008-8. PMID 16247600.

External links

Proteopedia page on histones

[Ranaudo_2026-1] 1 2 Ranaudo A, Miyake T, Cosentino U, Greco C (May 2026). "The double histone fold: Structure, functional implications across the tree of life and relevance to protein design". Protein Science. 35 (5) e70573. doi:10.1002/pro.70573. PMC 13088155. PMID 41994963.

[Slesarev_2001-2] Fahrner RL, Cascio D, Lake JA, Slesarev A (March 2001). "An ancestral nuclear protein assembly: crystal structure of the Methanopyrus kandleri histone". Protein Science. 10 (10): 2002–2007. doi:10.1110/ps.10901. PMC 2374223. PMID 11567091.

[Vanoni_2005-3] Greco C, Sacco E, Vanoni M, De Gioia L (October 2005). "Identification and in silico analysis of a new group of double-histone fold-containing proteins". Journal of Molecular Modeling. 12 (1): 76–84. doi:10.1007/s00894-005-0008-8. PMID 16247600.

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