Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Acipensins are antimicrobial peptides. Acipensins 1 and 2 have antibacterial activity against Gram-positive bacteria L.monocytogenes EGD (MIC are 1.1 uM and 1.0 uM, respectively) and S.aureus ATCC 33591 (MIC are 0.9 uM and 0.6 uM, respectively), against Gram-negative bacterium E.coli ML-35p (MIC are 0.7 uM and 0.3 uM, respectively) and antifungal activity against C.albicans 820 (MIC are 1.0 uM and 0.9 uM, respectively). Acipensin 6 has antibacterial activity against Gram-negative bacterium E.coli ML-35p (MIC=2.5 uM). Antimicrobial activity is reduced by high ionic strength. Acipensins 1, 2 and 6 have no hemolytic (up to 40 uM) or cytotoxic (up to 20 uM) effects on human cells in vitro. The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. Phosphorylation on Ser-2 is enhanced during mitosis. Phosphorylation on Ser-2 directly represses transcription. Acipensin 1. Acipensin 2. Acipensin 3. Acipensin 4. Acipensin 5. Acipensin 6. Belongs to the histone H2A family.