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Molecular and Cellular Biology, August 2001, p. 5223-5231, Vol. 21, No. 15
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.15.5223-5231.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

The Novel Transcription Factor e(y)2 Interacts with TAFII40 and Potentiates Transcription Activation on Chromatin Templates

Sofia Georgieva,1,2,3,4 Elena Nabirochkina,1,2 F. Jeffrey Dilworth,3 Holger Eickhoff,5 Peter Becker,4 Làszlò Tora,3 Pavel Georgiev,1 and Aleksey Soldatov1,5,*

Department of the Control of Genetic Processes, Institute of Gene Biology, Russian Academy of Sciences,1 and Center for Medical Studies of the University of Oslo at the Institute of Gene Biology,2 117334 Moscow, Russia; Institut de Genetique et de Biologie Moleculaire et Cellulaire, 67400 Illkirch, France3; and Molekularbiologie, Adolf-Butenandt-Institut, Ludwig-Maximilians-Universität München, 80336 Munich,4 and Max-Planck-Institut für Molekulare Genetik, 14195 Berlin,5 Germany

Received 2 May 2000/Returned for modification 12 June 2000/Accepted 5 April 2001

Weak hypomorph mutations in the enhancer of yellow genes, e(y)1 and e(y)2, of Drosophila melanogaster were discovered during the search for genes involved in the organization of interaction between enhancers and promoters. Previously, the e(y)1 gene was cloned and found to encode TAFII40 protein. Here we cloned the e(y)2 gene and demonstrated that it encoded a new ubiquitous evolutionarily conserved transcription factor. The e(y)2 gene is located at 10C3 (36.67) region and is expressed at all stages of Drosophila development. It encodes a 101-amino-acid protein, e(y)2. Vertebrates, insects, protozoa, and plants have proteins which demonstrate a high degree of homology to e(y)2. The e(y)2 protein is localized exclusively to the nuclei and is associated with numerous sites along the entire length of the salivary gland polytene chromosomes. Both genetic and biochemical experiments demonstrate an interaction between e(y)2 and TAFII40, while immunoprecipitation studies demonstrate that the major complex, including both proteins, appears to be distinct from TFIID. Furthermore, we provide genetic evidence suggesting that the carboxy terminus of dTAFII40 is important for mediating this interaction. Finally, using an in vitro transcription system, we demonstrate that recombinant e(y)2 is able to enhance transactivation by GAL4-VP16 on chromatin but not on naked DNA templates, suggesting that this novel protein is involved in the regulation of transcription.

* Corresponding author. Mailing address: Max-Planck-Institut für Molekulare Genetik, Abteilung Lehrach, Ihnestrasse 73, 14195 Berlin-Dahlem, Germany. Phone: 49-30-8413-1544. Fax: 49-30-8413-1380. E-mail: soldatov{at}molgen.mpg.de.

Molecular and Cellular Biology, August 2001, p. 5223-5231, Vol. 21, No. 15
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.15.5223-5231.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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