Histone H2A (78-86) RIIPRHLQL-acid


Histone 2A (H2A) which is one of the four core histones fundamental for compacting eukaryotic DNA into the nucleosome

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Catalogue number crb1001395
Sequence (one letter code) RIIPRHLQL-acid
Sequence (three letter code) H-Arg-Ile-Ile-Pro-Arg-His-Leu-Gln-Leu-OH
Purity >95%
Storage -20°C
Molecular Weight 1144.7

Hyland et al., (2005). Insights into the Role of Histone H3 and Histone H4 Core Modifiable Residues in Saccharomyces cerevisiae. Mol. Cell. Biol. (22) 10060. PMID: 16260619


Henneman et al., (2018). Structure and function of archaeal histones. PLoS One DOI: https://doi.org/10.1371/journal.pgen.1007582


Bönisch and Hake (2012). Histone H2A variants in nucleosomes and chromatin: more or less stable? Nucleic Acids Res. 40(21) 10719. PMID: 23002134

The histone H2A residues 78 to 86 are derived from histone 2A (H2A) which is one of the four core histones (H2A, H2B, H3 and H4) fundamental in compacting eukaryotic DNA into a structure known as the nucleosome. The nucleosome arises when 147 base pairs of DNA wrap around a H3-H4 tetramer and two H2A-H2B dimers, forming the histone octamer core.

At the site of DNA entry on the outer nucleosome, the C-terminus of H2A is present and is able to interact with linker histones or other factors. This allows for variation and changes in nucleosome stability to occur. Furthermore Histone H2A has histone variants such as H2A.Z and H2A.X (which are present in all organisms) and these variants alter the organisation of the DNA.

Due to histones containing a large number of lysine and arginine residues they have a positive net charge which interacts in an electrostatic manner with the negatively charged phosphate groups in DNA. The transcriptional activation or silencing of the chromatin is controlled by ATP-dependent chromatin remodelling factors and histone modifying enzymes which target histone proteins. Both processes function to alter to change the positioning of the nucleosome, allowing the DNA it to be either available to the transcription machinery or inaccessible.

Histone H2A (78-86)

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