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Human Molecular Genetics Advance Access published online on April 28, 2004
Human Molecular Genetics, doi:10.1093/hmg/ddh139
© 2004 by Oxford University Press
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Article

Ataxin-7 is a subunit of GCN5 histone acetyltransferase-containing complexes

Dominique Helmlinger 1, Sara Hardy 2, Souphatta Sasorith 3, Fabrice Klein 1, Flavie Robert 2, Chantal Weber 1, Laurent Miguet 4, Noëlle Potier 4, Alain Van-Dorsselaer 4, Jean-Marie Wurtz 3, Jean-Louis Mandel 1, Làszlò Tora 2, Didier Devys 1*

1 Department of Molecular Pathology, Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS/INSERM/ULP, BP 10142, 67404 Illkirch Cedex, France
2 Department of Transcription, Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS/INSERM/ULP, BP 10142, 67404 Illkirch Cedex, France
3 Department of Structural Genomics and Biology, Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS/INSERM/ULP, BP 10142, 67404 Illkirch Cedex, France
4 Laboratoire de Spectrométrie de Masse Bio-Organique, CNRS UMR7509 67087 Strasbourg, France

* To whom correspondence should be addressed. E-mail: devys{at}igbmc.u-strasbg.fr.


  Abstract

Spinocerebellar ataxia type 7 (SCA7) is a neurodegenerative disorder caused by a CAG repeat expansion in the SCA7 gene leading to elongation of a polyglutamine tract in ataxin-7, a protein of unknown function. A putative ataxin-7 yeast orthologue (SGF73) has been recently identified as a new component of the SAGA (Spt/Ada/Gcn5 acetylase) multisubunit complex, a coactivator required for transcription of a subset of RNA polymerase II-dependent genes. We show here that ataxin-7 is an integral component of mammalian SAGA-like complexes, the TATA-binding protein-free TAF-containing complex (TFTC) and the SPT3-TAF9-GCN5 acetyltransferase complex (STAGA). In agreement, immunoprecipitation of ataxin-7 retained a histone acetyltransferase activity characteristic for TFTC-like complexes. We further identified a minimal domain in ataxin-7 that is required for interaction with TFTC/STAGA subunits and is highly conserved through evolution, allowing the identification of a SCA7 gene family. We showed that this domain contains a conserved Cys3His motif that binds zinc, forming a new zinc-binding domain. Finally, polyglutamine expansion in ataxin-7 did not affect its incorporation into TFTC/STAGA complexes purified from SCA7 patient cells. We demonstrate here that ataxin-7 is the human orthologue of a the yeast SAGA SGF73 subunit and is a bona fide subunit of human TFTC-like transcriptional complexes.


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