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Nucleic Acids Research Advance Access originally published online on January 30, 2007
Nucleic Acids Research 2007 35(4):1134-1144; doi:10.1093/nar/gkl1168
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Nucleic Acids Research, 2007, Vol. 35, No. 4 1134-1144
© 2007 The Author(s).
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Molecular Biology

Sumoylation delays the ATF7 transcription factor subcellular localization and inhibits its transcriptional activity

Pierre-Jacques Hamard1, Michaël Boyer-Guittaut2, Barbara Camuzeaux1, Denis Dujardin1, Charlotte Hauss1, Thomas Oelgeschläger2, Marc Vigneron1, Claude Kedinger1 and Bruno Chatton1,*

1Institut Gilbert Laustriat, Ecole Supérieure de Biotechnologie de Strasbourg, UMR7175 CNRS-ULP, BP10413, 67412 Strasbourg Illkirch Cedex, France and 2Transcription laboratory, Marie Curie Research Institute, The Chart, Oxted, RH8 0TL, Surrey, England

*To whom correspondence should be addressed. Tel: +(33) 390 244 787; Fax +(33) 390 244 770; Email: bchatton{at}esbs.u-strasbg.fr

Received October 9, 2006. Revised December 21, 2006. Accepted December 21, 2006.

Over the past few years, small ubiquitin-like modifier (SUMO) modification has emerged as an important regulator of diverse pathways and activities including protein localization and transcriptional regulation. We identified a consensus sumoylation motif (IKEE), located within the N-terminal activation domain of the ATF7 transcription factor and thus investigated the role of this modification. ATF7 is a ubiquitously expressed transcription factor, homologous to ATF2, that binds to CRE elements within specific promoters. This protein is able to heterodimerize with Jun or Fos proteins and its transcriptional activity is mediated by interaction with TAF12, a subunit of the general transcription factor TFIID. In the present article, we demonstrate that ATF7 is sumoylated in vitro (using RanBP2 as a E3-specific ligase) and in vivo. Moreover, we show that ATF7 sumoylation affects its intranuclear localization by delaying its entry into the nucleus. Furthermore, SUMO conjugation inhibits ATF7 transactivation activity by (i) impairing its association with TAF12 and (ii) blocking its binding-to-specific sequences within target promoters.

The authors wish it to be known that, in their opinion the second and third authors contributed equally to this work.


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