This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Soutoglou, E. Articles by Tora, L. Search for Related Content PubMed PubMed Citation Articles by Soutoglou, E. Articles by Tora, L.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, May 2005, p. 4092-4104, Vol. 25, No. 10
0270-7306/05/$08.00+0     doi:10.1128/MCB.25.10.4092-4104.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

The Nuclear Import of TAF10 Is Regulated by One of Its Three Histone Fold Domain-Containing Interaction Partners

Evi Soutoglou, Màté A. Demény, Elisabeth Scheer, Giulia Fienga, Paolo Sassone-Corsi, and Làszlò Tora^*

Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), UMR 7104, Department of Transcriptional and Post-Transcriptional Control of Gene Regulation, BP 10142, 67404 Illkirch Cedex, CU de Strasbourg, France

Received 7 December 2004/ Returned for modification 19 January 2005/ Accepted 23 February 2005

TFIID, comprising the TATA box binding protein (TBP) and 13 TBP-associated factors (TAFs), plays a role in nucleation in the assembly of the RNA polymerase II preinitiation complexes on protein-encoding genes. TAFs are shared among other transcription regulatory complexes (e.g., SAGA, TBP-free TAF-containing complex [TFTC], STAGA, and PCAF/GCN5). Human TAF10, a subunit of both TFIID and TFTC, has three histone fold-containing interaction partners: TAF3, TAF8, and SPT7Like (SPT7L). In human cells, exogenously expressed TAF10 remains rather cytoplasmic and leptomycin B does not affect this localization. By using fluorescent fusion proteins, we show that TAF10 does not have an intrinsic nuclear localization signal (NLS) and needs one of its three interaction partners to be transported into the nucleus. When the NLS sequences of either TAF8 or SPT7L are mutated, TAF10 remains cytoplasmic, but a heterologous NLS can drive TAF10 into the nucleus. Experiments using fluorescence recovery after photobleaching show that TAF10 does not associate with any cytoplasmic partner but that once transported into the nucleus it binds to nuclear structures. TAF10 binding to importin ß in vitro is dependent on the coexpression of either TAF8 or TAF3, but not SPT7L. The cytoplasmic-nuclear transport of TAF10 is naturally observed during the differentiation of adult male germ cells. Thus, here we describe a novel role of the three mammalian interacting partners in the nuclear localization of TAF10, and our data suggest that a complex network of regulated cytoplasmic associations may exist among these factors and that this network is important for the composition of different TFIID and TFTC-type complexes in the nucleus.

---

* Corresponding author. Mailing address: Institut de Génétique et de Biologie Moléculaire et Cellulaire, UMR 7104, Department of Transcriptional and Post-Transcriptional Control of Gene Regulation, BP 10142, 67404 Illkirch Cedex, CU de Strasbourg, France. Phone: 33 388 65 34 44. Fax: 33 388 65 32 01. E-mail: laszlo{at}igbmc.u-strasbg.fr.

Present address: National Cancer Institute, NIH, 41 Library Drive, Bldg. 41 B507, Bethesda, MD 20892.

---

Molecular and Cellular Biology, May 2005, p. 4092-4104, Vol. 25, No. 10
0022-538X/05/$08.00+0     doi:10.1128/MCB.25.10.4092-4104.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

This article has been cited by other articles:

• Thomas, T., Dixon, M. P., Kueh, A. J., Voss, A. K. (2008). Mof (MYST1 or KAT8) Is Essential for Progression of Embryonic Development Past the Blastocyst Stage and Required for Normal Chromatin Architecture. Mol. Cell. Biol. 28: 5093-5105 [Abstract] [Full Text]  
• Verger, A., Quinlan, K. G. R., Crofts, L. A., Spano, S., Corda, D., Kable, E. P. W., Braet, F., Crossley, M. (2006). Mechanisms Directing the Nuclear Localization of the CtBP Family Proteins.. Mol. Cell. Biol. 26: 4882-4894 [Abstract] [Full Text]