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Human Molecular Genetics Advance Access originally published online on April 28, 2004
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Human Molecular Genetics, 2004, Vol. 13, No. 12 1257-1265
DOI: 10.1093/hmg/ddh139
Human Molecular Genetics, Vol. 13, No. 12 © Oxford University Press 2004; all rights reserved

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

Dominique Helmlinger1, Sara Hardy2, Souphatta Sasorith3, Fabrice Klein1, Flavie Robert2, Chantal Weber1, Laurent Miguet4, Noëlle Potier4, Alain Van-Dorsselaer4, Jean-Marie Wurtz3, Jean-Louis Mandel1, Làszlò Tora2 and Didier Devys1,*

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

Received February 16, 2004; Revised April 2, 2004; Accepted April 19, 2004

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 identified recently 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 the 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 conserved highly 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 the yeast SAGA SGF73 subunit and is a bona fide subunit of the human TFTC-like transcriptional complexes.

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


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