A histone fold is a structurally conserved

motif Motif may refer to: General concepts * Motif (chess composition), an element of a move in the consideration of its purpose * Motif (folkloristics), a recurring element that creates recognizable patterns in folklore and folk-art traditions * Moti ...

found near the

C-terminus The C-terminus (also known as the carboxyl-terminus, carboxy-terminus, C-terminal tail, C-terminal end, or COOH-terminus) is the end of an amino acid chain (protein or polypeptide), terminated by a free carboxyl group (-COOH). When the protein i ...

in every core

histone In biology, histones are highly basic proteins abundant in lysine and arginine residues that are found in eukaryotic cell nuclei. They act as spools around which DNA winds to create structural units called nucleosomes. Nucleosomes in turn ar ...

sequence in a

histone octamer A histone octamer is the eight-protein complex found at the center of a nucleosome core particle. It consists of two copies of each of the four core histone proteins ( H2A, H2B, H3, and H4). The octamer assembles when a tetramer, containing two ...

responsible for the binding of histones into

heterodimer In biochemistry, a protein dimer is a macromolecular complex formed by two protein monomers, or single proteins, which are usually non-covalently bound. Many macromolecules, such as proteins or nucleic acids, form dimers. The word ''dimer'' has ...

s. The histone fold averages about 70

amino acid Amino acids are organic compounds that contain both amino and carboxylic acid functional groups. Although hundreds of amino acids exist in nature, by far the most important are the alpha-amino acids, which comprise proteins. Only 22 alpha ...

s and consists of three

alpha helices The alpha helix (α-helix) is a common motif in the secondary structure of proteins and is a right hand-helix conformation in which every backbone N−H group hydrogen bonds to the backbone C=O group of the amino acid located four residues earli ...

connected by two short, unstructured loops. 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) via extensive hydrophobic interactions between each histone fold domain in a "handshake motif". Also the histone fold was first found in

TATA box In molecular biology, the TATA box (also called the Goldberg–Hogness box) is a sequence of DNA found in the core promoter region of genes in archaea and eukaryotes. The bacterial homolog of the TATA box is called the Pribnow box which ...

-binding protein-associated factors, which is a main component in

transcription Transcription refers to the process of converting sounds (voice, music etc.) into letters or musical notes, or producing a copy of something in another medium, including: Genetics * Transcription (biology), the copying of DNA into RNA, the fir ...

. The histone fold’s evolution can be found by different combinations of ancestral sets of

peptide Peptides (, ) are short chains of amino acids linked by peptide bonds. Long chains of amino acids are called proteins. Chains of fewer than twenty amino acids are called oligopeptides, and include dipeptides, tripeptides, and tetrapeptides. ...

s that make up helix-strand-helix motif that come from the three folds from the ancestral fragments. These peptide chains can be found in the archaeal histones, which could have come from eukaryotic H3-H4 tetramer. The archaeal single-chain histones are also found in the bacterium

Aquifex aeolicus "''Aquifex aeolicus''" is a chemolithoautotrophic, Gram-negative, motile, hyperthermophilic bacterium. "''A. aeolicus"'' is generally rod-shaped with an approximate length of 2.0-6.0μm and a diameter of 0.4-0.5μm. "''A. aeolicus''" is neither ...

. Which helps the diverse bacteria phylogeny coming from the ancestry of eukaryotes and archaea with lateral gene transfers to get to the bacteria. These lead into the octamer articulated protein endoskeleton for DNA compaction. From this endoskeleton it has a central segment that folds for the histone dimerization. This then leads into the end segments of the fold to make properties of dimer-dimer contacts that also cap the protein super helix at the octamer. One species that looked at is

Drosophila ''Drosophila'' () is a genus of flies, belonging to the family Drosophilidae, whose members are often called "small fruit flies" or (less frequently) pomace flies, vinegar flies, or wine flies, a reference to the characteristic of many s ...

, and in the subunits of the Drosophila transcription initiation factor has specific amino acid sequences that have different characteristics of the histone folds that make up the two proteins make up the subunits. When just looking at the histone fold motif in the Drosophila the protein-protein and the protein DNA interaction of the core histone proteins can be found by looking at the non-histone proteins. This can then be used in “Structural studies on the TAFII42/TAFII62 complex from Drosophila and HMfB from

Methanococcus ''Methanococcus'' is a genus of coccoid methanogens of the family Methanococcaceae. They are all mesophiles, except the thermophilic '' M. thermolithotrophicus'' and the hyperthermophilic '' M. jannaschii''. The latter was discovered at the b ...

fervidus, proteins identified as containing the histone fold in the aforementioned searches, confirmed that a histone-like substructure exists in these proteins, with the individual proteins folding into the canonical histone fold motif”. The evolutionary structure and range of the histone protein-protein and DNA-protein interactions of the histone fold proteins has a very wide range of evolutionary traits that form the structures and other proteins. Histone folds play a role in the nucleosomal core particle by conserving histone interactions when looking at interface surfaces. These contain more than one histone fold. The structure of the nucleosome core particle has two modes that have the largest interaction surfaces with are in groups H3-H4 and H2A-H2B heterotypic dimer interactions. When looking at the H2A-H2A structure it has a modification of the loop at the interface that excludes it from clustering with the same interface of other structures. Which makes it have a different function in the transcriptional activation. Also the two modes are distinct due to having the longest helix chains. These use the handshake interactions between the two histone folds, while they also use it to make themselves unique comparted to the rest of the modes. Similarly modes 5 and 7 of the core nucleosome particle use two types of histone fold dimers which show that all histone domains share a similar structural motif to be able to be able to interact with one another and to interact in different ways. Showing how flexible and adaptive the structure of histones are. H4 and H2A can form an internucleosomal contacts that can be

acetylated : In organic chemistry, acetylation is an organic esterification reaction with acetic acid. It introduces an acetyl group into a chemical compound. Such compounds are termed ''acetate esters'' or simply ''acetates''. Deacetylation is the opposit ...

to be able to perform ionic interactions between two peptides, which in turn could change the surrounding internucleosomal contacts that can make a way to opening the

chromatin Chromatin is a complex of DNA and protein found in eukaryote, eukaryotic cells. The primary function is to package long DNA molecules into more compact, denser structures. This prevents the strands from becoming tangled and also plays important ...

References

Protein folding Molecular biology {{Biochem-stub