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EpiCypher
Mononucleosomes assembled from recombinant human histones expressed in E. coli (two each of histones H2A*, H2B, H3 and H4; accession numbers: H2A-P04908*; H2B-O60814; H3.1-P68431; H4-P62805) wrapped by 147 base pairs of 601 positioning sequence DNA [1] containing a 5’ biotin-TEG group. *Histone H2A contains a glutamate-to-alanine (E-to-A) substitution at position 61 (H2AE61A). H2AE61A is among key residues forming a negatively charged region on the nucleosome surface named the “acidic patch”. The acidic patch is a conserved interaction hub for neighboring nucleosomes and nucleosome binding proteins, often via salt bridges with arginine anchors, and is functionally critical in chromatin condensation and chromatin remodeling [2-4]. H2AE61 resides in the alpha2 helix and forms a key salt bridge with H4K16. H2AE61 mediates chromatin binding with factors such as LANA, RCC1, IL-33, SIR3 and HMGN2 [2]. H2AE61A disrupts chromatin remodeling by the ISWI remodeler SNF2h [4].
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