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HDAC6-induced premature chromatin compaction in mouse oocytes and fertilised eggs

Published online by Cambridge University Press:  08 March 2004

André Verdel ,
Daphné Seigneurin-Berny ,
Anne-Karen Faure ,
Mina Eddahbi ,
Saadi Khochbin  and
Stefan Nonchev
André Verdel
Affiliation:
Institute Albert Bonniot, INSERM U309, La Tronche, France Present address: Harvard Medical School, LHRRB Room 517, Department of Cell Biology, 240 Longwood Avenue, Boston, MA 02115-5730, USA
Daphné Seigneurin-Berny
Affiliation:
Institute Albert Bonniot, INSERM U309, La Tronche, France Present address: Laboratoire de Physiologie Cellulaire Vegetale, UMR 5019, Departement de Biologie Moleculaire et Structurale, Grenoble, France
Anne-Karen Faure
Affiliation:
Institute Albert Bonniot, INSERM U309, La Tronche, France
Mina Eddahbi
Affiliation:
Institute Albert Bonniot, INSERM U309, La Tronche, France
Saadi Khochbin
Affiliation:
Institute Albert Bonniot, INSERM U309, La Tronche, France
Stefan Nonchev
Affiliation:
Institute Albert Bonniot, INSERM U309, La Tronche, France
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Abstract

Chromatin remodelling in the fertilised mouse egg is intimately linked to protein synthesis and degradation, to protamine by histone replacement and to specific histone modifications. The involvement of histone deacetylases (HDACs) in the beginning of development is poorly understood. HDACs are essential for cell proliferation and in the control of gene expression in a wide variety of mammalian systems. Here we focus on mHDAC6, a recently identified class II histone deacetylase, and we analyse its expression and localisation in oocytes and pronuclear zygotes. By indirect immunofluorescence we show that mHDAC6 is detected in the cytoplasm of germinal vesicle (GV) stage oocytes and 1-cell embryos. Ectopic expression of this enzyme after injection into germinal vesicles and pronuclei alters the nuclear structure and causes premature compaction of the chromatin. Our data suggest that the effect of condensation is linked to the ubiquitin-binding activity of mHDAC6, rather than to its function as a deacetylase.

Type
Research Article
Information
Zygote , Volume 11 , Issue 4 , November 2003 , pp. 323 - 328
Copyright
2003 Cambridge University Press

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