Hsp56 mRNA in Paracentrotus lividus embryos binds to a mitochondrial protein

Authors

  • Carlo Maria Di Liegro,

    1. Dipartimento di Biologia Cellulare e dello Sviluppo “A. Monroy”, Università di Palermo, Viale delle Scienze, Parco d'Orleans, 90128 Palermo, Italy
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  • Anna Maria Rinaldi

    Corresponding author
    1. Dipartimento di Biologia Cellulare e dello Sviluppo “A. Monroy”, Università di Palermo, Viale delle Scienze, Parco d'Orleans, 90128 Palermo, Italy
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Corresponding author. Fax: +39 0916577430. rinaldi@unipa.it

Abstract

We previously demonstrated that Paracentrotus lividus Hsp56 mitochondrial chaperonin is constitutively expressed during development, that it has a specific territorial distribution, both in normal and heat-shocked embryos, and that its amount increases after heat shock [Roccheri MC, Patti M, Agnello M, Gianguzza F, Carra E, Rinaldi AM. Localization of mitochondrial Hsp56 chaperonin during sea urchin development. Biochem Biophys Res Commun 2001;287:1093–98] and cadmium treatment [Roccheri MC, Agnello M, Boneventura R, Matranga V. Cadmium induces the expression of specific stress proteins in sea urchin embryos. Biochem Biophys Res Commun 2004;321:80–7]. In this study, we looked at Hsp56 mRNA during normal development and under stress conditions. The messenger is almost constantly expressed at all stages of development and its amount is steadily increased in stressed embryos. Moreover, we found, using T1 RNase protection assay, that the most proximal region of the 3′-UTR of the Hsp56 mRNA binds a 40 kDa protein: this factor is more abundant in the mitochondrial extract and, more specifically, in the outer membrane of the organelle.

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