Abstract:

Cdyl (chromodomain-Y-like) is a chromodomain-containing protein that is predominantly expressed during mouse spermiogenesis. In its carboxy-terminal portion, there is a domain with homology to the coenzyme A (CoA) pocket of the enoyl-CoA hydratase/isomerase, which is shown here to be able to bind CoA and histone deacetylases (HDACs). It also efficiently represses transcription. Moreover, the binding of Hdac1 represses the ability of Cdyl to bind CoA, and a Cdyl-CoA interaction only occurs in the absence of HDACs. These data suggest that Cdyl is primarily a transcriptional co-repressor. However, the degradation of cellular Hdac1 and Hdac2, as observed here in the elongating spermatids, may provide an HDAC-free environment in which Cdyl could bind CoA and participate in the global chromatin remodelling that occurs in these cells.

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Cdyl: a new transcriptional co-repressor

Cécile Caron

Christophe Pivot-Pajot

^{Laboratoire de Biologie Moléculaire et Cellulaire de la Différenciation—INSERM U309, Equipe Chromatine et Expression des Gènes, Institut Albert Bonniot, Faculté de Médecine de Grenoble, Domaine de la Merci, 38706 La Tronche Cedex, France}

^{Department of Developmental Biology, Flanders Interuniversity Institute for Biotechnology and Laboratory of Molecular Biology, University of Leuven, Herestraat 49, B-3000 Leuven, Belgium}

^{Tel: +33 4 76 54 95 83; Fax: +33 4 76 54 95 95;}rf.elbonerg-fju@nibhcohk

Received 2003 Mar 26; Revised 2003 Jun 23; Accepted 2003 Jul 10.

Abstract

Cdyl (chromodomain-Y-like) is a chromodomain-containing protein that is predominantly expressed during mouse spermiogenesis. In its carboxy-terminal portion, there is a domain with homology to the coenzyme A (CoA) pocket of the enoyl-CoA hydratase/isomerase, which is shown here to be able to bind CoA and histone deacetylases (HDACs). It also efficiently represses transcription. Moreover, the binding of Hdac1 represses the ability of Cdyl to bind CoA, and a Cdyl–CoA interaction only occurs in the absence of HDACs. These data suggest that Cdyl is primarily a transcriptional co-repressor. However, the degradation of cellular Hdac1 and Hdac2, as observed here in the elongating spermatids, may provide an HDAC-free environment in which Cdyl could bind CoA and participate in the global chromatin remodelling that occurs in these cells.

Abstract

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Acknowledgments

We are grateful to D. Allis, S. Khorasanizadeh and B. Lahn for helpful discussions, to E. Seto for the gift of FLAG–Hdac1 and FLAG–Hdac2, and to Y. Shi for the gift of the CtBP siRNA plasmid. We are also grateful to S. Curtet and R. Iratni for technical assistance. This work was supported by the INSERM Assistance Médicale à la Procréation and Région Rhône-Alpes 'émergence' programmes. C.C. is supported by the INSERM 'délégation' programme and L.A.v.G. by a postdoctoral fellowship from the Fund for Scientific Research Flanders, and he thanks D. Huylebroeck for support.

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