DNA compaction by polyaminic cations and proteins involves reversible condensation mechanisms. Polyamines, metal cations, and histone proteins are utilized to compact lengthy DNA chains. Chromatin organization begins with nucleosomal arrays, further compacted by linker histones. Various factors such as DNA methylation, histone modifications, and non-histone proteins influence chromatin structure. Posttranslational modifications like acetylation and methylation alter nucleosome shape. Polyamines induce significant phase transitions, while cationic surfactants drive conformational changes in DNA. In sperm cells, protamines replace histones, leading to dense DNA packing. Despite advances, unresolved aspects persist in understanding the dynamic regulation of chromatin structure, highlighting avenues for future research. An overview of current knowledge and cutting-edge discoveries in the field of reversible DNA compaction induced by charged polyamines and histone proteins is presented in this work, highlighting emerging mechanisms of chromatin compaction and their relevance to cellular function, disease, and potential therapeutic strategies.
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