![]() ![]() Journal of Biological Chemistry, 2003, vol. Although the association of histones with nucleoplasmin may involve some ionic interactions, the interaction process is not electrostatically driven. These results indicate that interactions other than those electrostatic in nature (likely hydrophobic) also play a critical role in the formation of the complex between the negatively charged nucleoplasmin and positively charged histones. Removal of the histone N-terminal 'tail' domains or the major C-terminal polyglutamic tracts of nucleoplasmin did not alter these binding properties. To better understand the latter process, we have used sedimentation velocity, sedimentation equilibrium, and sucrose gradient fractionation analysis to show that the pentameric form of nucleoplasmin binds to a histone octamer equivalent consisting of equal amounts of the four core histones, H2A, H2B, H3, and H4, without any noticeable preference for any of these proteins. This molecule has been shown to be responsible for the removal of the sperm-specific proteins and deposition of somatic histones onto the male pronuclear chromatin. Nucleoplasmin is one of the most abundant proteins in Xenopus laevis oocytes, and it has been involved in the chromatin remodeling that takes place immediately after fertilization. Interaction of nucleoplasmin with core histonesĪmerican Society for Biochemistry and Molecular Biology We also report the in-solution structures of HDT2 pentamers in complex with histone oligomers. The term molecular chaperone was coined to describe its role in the. Please use this identifier to cite or link to this item: The HDT-NTD requires an additional A2 acidic tract C-terminal to the nucleoplasmin domain for interaction with histone H3/H4 and H2A/H2B oligomers. Nucleoplasmin is the most abundant nuclear protein in Xenopus oocytes and eggs. ![]()
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