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Hsp90 prevents phenotypic variation by suppressing the mutagenic activity of transposons

Author

Listed:
  • Valeria Specchia

    (University of Salento)

  • Lucia Piacentini

    (Istituto Pasteur, University of Rome ‘La Sapienza’)

  • Patrizia Tritto

    (University of Bari)

  • Laura Fanti

    (Istituto Pasteur, University of Rome ‘La Sapienza’)

  • Rosalba D’Alessandro

    (University of Bari)

  • Gioacchino Palumbo

    (University of Bari)

  • Sergio Pimpinelli

    (Istituto Pasteur, University of Rome ‘La Sapienza’)

  • Maria P. Bozzetti

    (University of Salento)

Abstract

Hsp90 as a suppressor of phenotypic variation It has been suggested that the molecular chaperone protein Hsp90 (heat shock protein 90) is part of an evolutionarily conserved buffering mechanism that preserves the development process from phenotypic variance despite genetic and environmental perturbation. Specchia et al. offer an additional or an alternative mechanism whereby Hsp90 influences phenotypic variation by affecting the piRNA silencing mechanism leading to transposon activation.

Suggested Citation

  • Valeria Specchia & Lucia Piacentini & Patrizia Tritto & Laura Fanti & Rosalba D’Alessandro & Gioacchino Palumbo & Sergio Pimpinelli & Maria P. Bozzetti, 2010. "Hsp90 prevents phenotypic variation by suppressing the mutagenic activity of transposons," Nature, Nature, vol. 463(7281), pages 662-665, February.
    • Handle: RePEc:nat:nature:v:463:y:2010:i:7281:d:10.1038_nature08739
    DOI: 10.1038/nature08739
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