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Journal of Cellular Biochemistry

Functional studies of MP62 during male chromatin decondensation in sea urchins

Authors

  • Claudio Iribarren,

    1. Department of Biochemistry and Molecular Biology, Universidad de Concepción, Concepción, Chile
    2. Department of Basical Sciences, Universidad Santo Tomas, Concepción, Chile
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  • Viviana Hermosilla,

    1. Department of Biochemistry and Molecular Biology, Universidad de Concepción, Concepción, Chile
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  • Violeta Morin,

    1. Department of Biochemistry and Molecular Biology, Universidad de Concepción, Concepción, Chile
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  • Marcia Puchi

    Corresponding author
    1. Department of Biochemistry and Molecular Biology, Universidad de Concepción, Concepción, Chile
    2. Department of Biological Sciences, Universidad Andrés Bello, Concepción, Chile
    • Departamento de Ciencias Biológicas, Facultad de Ciencias Biológicas, Universidad Andrés Bello, Concepción, Chile.
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Abstract

In amphibians, sperm histone transition post-fertilization during male pronucleus formation is commanded by histone chaperone Nucleoplasmin (NPM). Here, we report the first studies to analyze the participation of a Nucleoplasmin-like protein on male chromatin remodeling in sea urchins. In this report, we present the molecular characterization of a nucleoplasmin-like protein that is present in non fertilized eggs and early zygotes in sea urchin specie Tetrapygus niger. This protein, named MP62 can interact with sperm histones in vitro. By male chromatin decondensation assays and immunodepletion experiments in vitro, we have demonstrated that this protein is responsible for sperm nucleosome disorganization. Furthermore, as amphibian nucleoplasmin MP62 is phosphorylated in vivo immediately post-fertilization and this phosphorylation is dependent on CDK-cyclin activities found after fertilization. As we shown, olomoucine and roscovitine inhibits male nucleosome decondensation, sperm histone replacement in vitro and MP62 phosphorylation in vivo. This is the first report of a nucleoplasmin-like activity in sea urchins participating during male pronucleus formation post-fecundation. J. Cell. Biochem. 114: 1779–1788, 2013. © 2013 Wiley Periodicals, Inc.

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