Hsp90 prevents phenotypic variation by suppressing the mutagenic activity of transposons

Valeria Specchia, Lucia Piacentini, Patrizia Tritto, Laura Fanti, Rosalba D’Alessandro, Gioacchino Palumbo, Sergio Pimpinelli and Maria P. Bozzetti ()
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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

Nature, 2010, vol. 463, issue 7281, 662-665

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.

Date: 2010
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DOI: 10.1038/nature08739

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