A Quantitative Characterization of Nucleoplasmin/Histone Complexes Reveals Chaperone Versatility

• DOI: 10.1038/srep32114
• Publication Date: 2016-08-25T09:37:12Z
• Authors: Noelia Fernández-...; Aitor Franco; Adrian Velázquez-...; Edurne Alonso; Arturo Muga; Adelina Prado
• Keywords: Chaperone (clinical); Histone H2B; Histone code; Linker

Abstract Nucleoplasmin (NP) is an abundant histone chaperone in vertebrate oocytes and embryos involved storing releasing maternal histones to establish maintain the zygotic epigenome. NP has been considered a H2A–H2B recently it shown that can also interact with H3-H4. However, its interaction different types of not quantitatively studied so far. We show here binds H2A–H2B, H3-H4 linker K d values subnanomolar range, forming complexes. Post-translational modifications regulate exposure polyGlu tract at disordered distal face protein induce increase affinity for all histones. The relative fact they could explain their competition binding, relevant process NP-mediated sperm chromatin remodelling during fertilization. Our data tetramers nucleosomal conformation dimers, transferring them DNA form disomes tetrasomes. This finding might be elucidate role disassembly assembly replication transcription.