12/9/2023 0 Comments Nucleoplasmin![]() ( C) Glycerol density gradient of HeLa cell nuclear extracts. Images were observed under confocal microscopy. HeLa cells were subjected to immunofluorescence analysis using anti-NPM1 and anti-NPM3 antibodies. ( B) Localization of endogenous NPM1 and NPM3 in HeLa cells. EF, EF–NPM1, EF–NPM2 and EF–NPM3 were transiently expressed in HeLa cells and the localization of EGFP proteins was examined by fluorescent microscopy. ( A) Localization of EGFP-tagged NPM proteins. Our results proposed a novel mechanism whereby three NPM proteins cooperatively regulate chromatin disassembly and assembly in the early embryo and in somatic cells.Īssociation between human NPM proteins. NPM3 also suppressed the RNA-binding activity of NPM1, which enhanced the nucleoplasm-nucleolus shuttling of NPM1 in somatic cell nuclei. Furthermore, the oligomer formation with NPM1 elicited NPM3 nucleosome assembly and sperm chromatin decondensation activity. Maximal sperm chromatin remodeling activity of NPM2 required the inhibition of its non-specific nucleic acid-binding activity by phosphorylation. NPM1 and NPM2 mediated nucleosome assembly independently of other NPM proteins, whereas the function of NPM3 was largely dependent on formation of a complex with NPM1. We characterized the sperm chromatin decondensation and nucleosome assembly activities of three human NPM proteins. In mammals, three nucleoplasmin/nucleophosmin (NPM) family proteins-NPM1, NPM2 and NPM3-expressed in oocytes are presumed to cooperatively regulate sperm chromatin remodeling. This reaction involves the removal of sperm-specific basic proteins and chromatin assembly with histones. Sperm chromatin remodeling after oocyte entry is the essential step that initiates embryogenesis. ![]()
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