Nucleosome, Recombinant Human, Acidic Patch Mutant H2AE92K Biotinylated

Recombinant mononucleosomes consist of 147 base pairs of DNA wrapped around an octamer core of histone proteins (two each of H2A, H2B, H3.1, and H4) to form a nucleosome, the basic repeating unit of chromatin. The 147 bp 601 sequence containing a 5’ biotin-TEG group has high affinity for histone octamers and is useful for nucleosome assembly [1]. Histone H2A contains a glutamate-to-lysine (E-to-K) substitution at position 92 (H2AE92K). H2AE92 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]. H2AE92 resides in the H2A C-terminal extension and is associated with nucleosome binding factors such as histone H4 N-terminal tail, LANA, RCC1, IL-33, SIR3, HMGN2, and remodeling ATPases [2-4]. H2AE92K disrupts binding with SMARCB1 [5].