Molecular and Cellular Biology, January 2001, p. 614-623, Vol. 21, No. 2
0270-7306/01/$04.00+0 DOI: 10.1128/MCB.21.2.614-623.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Instituto Cajal, C.S.I.C., Madrid 28002, Spain
Received 6 July 2000/Returned for modification 29 August 2000/Accepted 16 October 2000
The transcription factor TFIID is a multiprotein complex that includes the TATA box binding protein (TBP) and a number of associated factors, TAFII. Prodos (PDS) is a conserved protein that exhibits a histone fold domain (HFD). In yeast two-hybrid tests using PDS as bait, we cloned the Drosophila TAFII, dTAFII16, as a specific PDS target. dTAFII16 is closely related to human TAFII30 and to another recently discovered Drosophila TAF, dTAFII24. PDS and dTAFII24 do not interact, however, thus establishing a functional difference between these dTAFs. The PDS-dTAFII16 interaction is mediated by the HFD motif in PDS and the N terminus in dTAFII16, as indicated by yeast two-hybrid assays with protein fragments. Luciferase-reported transcription tests in transfected cells show that PDS or an HFD-containing fragment activates transcription only with the help of dTAFII16 and TBP. Consistent with this, the eye phenotype of flies expressing a sev-Ras1 construct is modulated by PDS and dTAFII16 in a gene dosage-dependent manner. Finally, we show that PDS function is required for cell viability in somatic mosaics. These findings indicate that PDS is a novel transcriptional coactivator that associates with a member of the general transcription factor TFIID.
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