<p>Histone proteins have central roles in both chromatin organisation (asstructural units of the nucleosome) and gene regulation (as dynamic componentsthat have a direct impact on DNA transcription and replication). EukaryoticDNA wraps around a histone octamer to form a nucleosome, the first order ofcompaction of eukaryotic chromatin. The core histone octamer is composed of acentral H3-H4 tetramer and two flanking H2A-H2B dimers. Each of the corehistone contains a common structural motif, called the histone fold, whichfacilitates the interactions between the individual core histones.</p> <p>In addition to the core histones, there is a "linker histone" called H1 (or H5 in avian species). The linker histones present in all multicellular eukaryotes are the most divergent group of histones, with numerous cell type- and stage-specific variant. Linker histone H1 is an essential component of chromatin structure. H1 links nucleosomes into higher order structures.Histone H5 performs the same function as histone H1, and replaces H1 in certain cells. The structure of GH5, the globular domain of the linker histone H5 is known [<cite idref="PUB00004142"/>, <cite idref="PUB00004625"/>]. The fold is similar to the DNA-binding domain of the catabolite gene activator protein, CAP, thus providing a possible model for the binding of GH5 to DNA.</p><p>The linker histones, which do not contain the histone fold motif, are critical to the higher-order compaction of chromatin, because they bind to internucleosomal DNA and facilitate interactions between individual nucleosomes. In addition, H1 variants have been shown to be involved in the regulation of developmental genes. A common feature of this protein family is a tripartite structure in which a globular (H15) domain of about 80 amino acids is flanked by two less structured N- and C-terminal tails. The H15domain is also characterised by high sequence homology among the family oflinker histones. The highly conserved H15 domain is essential for the bindingof H1 or H5 to the nucleosome. It consists of a three helix bundle (I-III),with a beta-hairpin at the C terminus. There is also a short three-residuestretch between helices I and II that is in the beta-strand conformation.Together with the C-terminal beta-hairpin, this strand forms the third strandof an antiparallel beta-sheet [<cite idref="PUB00055532"/>, <cite idref="PUB00004142"/>, <cite idref="PUB00055533"/>, <cite idref="PUB00031779"/>].</p><p>Proteins known to contain a H15 domain are: <ul><li>- Eukaryotic histone H1. The histones H1 constitute a family with many variants, differing in their affinity for chromatin. Several variants are simultaneously present in a single cell. For example, the nucleated erythrocytes of birds contain both H1 and H5, the latter being an extreme variant of H1.</li><li> - Eukaryotic MHYST family of histone acetyltransferase. Histone acetyltransferases transfer an acetyl group from acetyl-CoA to the epsylon- amino group of lysine within the basic NH2-termini of histones, which bind the acidic phosphates of DNA [<cite idref="PUB00055534"/>].</li> </ul></p><p> This entry represents the H15 domain.</p>