Interaction of Nucleoplasmin with Core Histones
Autor: | Juan Ausió, Carme Arnan, Manel Chiva, Cèlia Prieto, Núria Saperas |
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Rok vydání: | 2003 |
Předmět: |
Nucleoplasmin
Somatic cell Xenopus Biology Biochemistry Chromatin remodeling Histones Xenopus laevis Animals Nucleoproteïnes Histone octamer Nucleoplasmins education Molecular Biology education.field_of_study urogenital system Nuclear Proteins Cell Biology Phosphoproteins biology.organism_classification Molecular biology Chromatin Metabolisme Protein Structure Tertiary Nucleoproteins Metabolism Histone Sedimentation equilibrium Biophysics biology.protein Hydrophobic and Hydrophilic Interactions Protein Binding |
Zdroj: | Dipòsit Digital de la UB Universidad de Barcelona |
ISSN: | 0021-9258 |
Popis: | 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. 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. 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. Removal of the histone N-terminal 'tail' domains or the major C-terminal polyglutamic tracts of nucleoplasmin did not alter these binding properties. 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. Although the association of histones with nucleoplasmin may involve some ionic interactions, the interaction process is not electrostatically driven. |
Databáze: | OpenAIRE |
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