HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 280, Issue 11, 9937-9945, March 18, 2005

This Article Full Text Full Text (PDF) All Versions of this Article: 280/11/9937    most recent M414149200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Boyer-Guittaut, M. Articles by Oelgeschläger, T. Search for Related Content PubMed PubMed Citation Articles by Boyer-Guittaut, M. Articles by Oelgeschläger, T. Social Bookmarking                      What's this?

SUMO-1 Modification of Human Transcription Factor (TF) IID Complex Subunits

INHIBITION OF TFIID PROMOTER-BINDING ACTIVITY THROUGH SUMO-1 MODIFICATION OF hsTAF5^*

Michaël Boyer-Guittaut, Kivanç Birsoy, Corinne Potel¶, Gill Elliott¶, Ellis Jaffray||, Joanna M. Desterro||**, Ron T. Hay||, and Thomas Oelgeschläger

From the Transcription Laboratory and the ^¶Virus Assembly Laboratory, Marie Curie Research Institute, Oxted, Surrey RH8 0TL and the ^||Centre for Biomolecular Sciences, University of St. Andrews, North Haugh, St. Andrews KY16 9ST, United Kingdom

The TFIID complex is composed of the TATA-binding protein (TBP) and TBP-associated factors (TAFs) and is the only component of the general RNA polymerase II (RNAP II) transcription machinery with intrinsic sequence-specific DNA-binding activity. Binding of transcription factor (TF) IID to the core promoter region of protein-coding genes is a key event in RNAP II transcription activation and is the first and rate-limiting step of transcription initiation complex assembly. Intense research efforts in the past have established that TFIID promoter-binding activity as well as the function of TFIID-promoter complexes is tightly regulated through dynamic TFIID interactions with positive- and negative-acting transcription regulatory proteins. However, very little is known about the role of post-translational modifications in the regulation of TFIID. Here we show that the human TFIID subunits hsTAF5 and hsTAF12 are modified by the small ubiquitin-related modifier SUMO-1 in vitro and in human cells. We identify Lys-14 in hsTAF5 and Lys-19 in hsTAF12 as the primary SUMO-1 acceptor sites and show that SUMO conjugation has no detectable effect on nuclear import or intranuclear distribution of hsTAF5 and hsTAF12. Finally, we demonstrate that purified human TFIID complex can be SUMO-1-modified in vitro at both hsTAF5 and hsTAF12. We find that SUMO-1 conjugation at hsTAF5 interferes with binding of TFIID to promoter DNA, whereas modification of hsTAF12 has no detectable effect on TFIID promoter-binding activity. Our observations suggest that reversible SUMO modification at hsTAF5 contributes to the dynamic regulation of TFIID promoter-binding activity in human cells.

Received for publication, December 16, 2004

^* This work was supported by Marie Curie Cancer Care and by a project grant from the Association of International Cancer Research. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Present address: Laboratory of Metabolic Diseases, The Rockefeller University, New York, NY 10021.

^** Present address: Institute of Molecular Medicine, Faculty of Medicine, University of Lisbon, 1649-028 Lisbon, Portugal.

To whom correspondence should be addressed: Transcription Laboratory, Marie Curie Research Institute, The Chart, Oxted, Surrey RH8 0TL, United Kingdom. Tel.: 44-1883-722-306; Fax: 44-1883-714-375; E-mail: t.oelgeschlager{at}mcri.ac.uk.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				A. Voulgari, S. Voskou, L. Tora, I. Davidson, T. Sasazuki, S. Shirasawa, and A. Pintzas TATA Box-Binding Protein-Associated Factor 12 Is Important for RAS-Induced Transformation Properties of Colorectal Cancer Cells Mol. Cancer Res., June 1, 2008; 6(6): 1071 - 1083. [Abstract] [Full Text] [PDF]

				A. Jakobs, F. Himstedt, M. Funk, B. Korn, M. Gaestel, and R. Niedenthal Ubc9 fusion-directed SUMOylation identifies constitutive and inducible SUMOylation Nucleic Acids Res., September 27, 2007; 35(17): e109 - e109. [Abstract] [Full Text] [PDF]

				C.-C. Chou, C. Chang, J.-H. Liu, L.-F. Chen, C.-D. Hsiao, and H. Chen Small Ubiquitin-like Modifier Modification Regulates the DNA Binding Activity of Glial Cell Missing Drosophila Homolog a J. Biol. Chem., September 14, 2007; 282(37): 27239 - 27249. [Abstract] [Full Text] [PDF]

				P.-J. Hamard, M. Boyer-Guittaut, B. Camuzeaux, D. Dujardin, C. Hauss, T. Oelgeschlager, M. Vigneron, C. Kedinger, and B. Chatton Sumoylation delays the ATF7 transcription factor subcellular localization and inhibits its transcriptional activity Nucleic Acids Res., February 28, 2007; 35(4): 1134 - 1144. [Abstract] [Full Text] [PDF]

				Y. Sato, K. Miyake, H. Kaneoka, and S. Iijima Sumoylation of CCAAT/Enhancer-binding Protein {alpha} and Its Functional Roles in Hepatocyte Differentiation J. Biol. Chem., August 4, 2006; 281(31): 21629 - 21639. [Abstract] [Full Text] [PDF]

				V. Chung, B. Zhou, X. Liu, L. Zhu, L. M. Boo, H.-V. Nguyen, D. K. Ann, J. Song, Y. Chen, and Y. Yen SUMOylation plays a role in gemcitabine- and bortezomib-induced cytotoxicity in human oropharyngeal carcinoma KB gemcitabine-resistant clone. Mol. Cancer Ther., March 1, 2006; 5(3): 533 - 540. [Abstract] [Full Text] [PDF]

				J. Anckar, V. Hietakangas, K. Denessiouk, D. J. Thiele, M. S. Johnson, and L. Sistonen Inhibition of DNA Binding by Differential Sumoylation of Heat Shock Factors Mol. Cell. Biol., February 1, 2006; 26(3): 955 - 964. [Abstract] [Full Text] [PDF]