Nucleosome, Recombinant Human, Acidic Patch Mutant H2AE61A 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-alanine (E-to-A) substitution at position 61 (H2AE61A). H2AE61 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 SMARCA5/SNF2h [4].