A. Hernandez-hernandez et A. Ferrus, Prodos is a conserved transcriptional regulator that interacts with dTAF(II)16 in Drosophila melanogaster, MOL CELL B, 21(2), 2001, pp. 614-623
The transcription factor TFIID is a multiprotein complex that includes the
TATA box binding protein (TBP) and a number of associated factors, TAF(II).
Prodos (PDS) is a conserved protein that exhibits a histone fold domain (H
FD). In yeast two-hybrid tests using PDS as bait, we cloned the Drosophila
TAF(II), dTAF(II)16, as a specific PDS target. dTAF(II)16 is closely relate
d to human TAF(II)30 and to another recently discovered Drosophila TAF, dTA
F(II)24. PDS and dTAF(II)24 do not interact, however, thus establishing a f
unctional difference between these dTAFs. The PDS-dTAF(II)16 interaction is
mediated by the HFD motif in PDS and the N terminus in dTAF(II)16, as indi
cated by yeast two-hybrid assays with protein fragments. Luciferase-reporte
d transcription tests in transfected cells show that PDS or an HFD-containi
ng fragment activates transcription only with the help of dTAF(II)16 and TB
P. Consistent with this, the eye phenotype of flies expressing a sev-Ras1 c
onstruct is modulated by PDS and dTAF(II)16 in a gene dosage-dependent mann
er. Finally, we show that PDS function is required for cell viability in so
matic mosaics. These findings indicate that PDS is a novel transcriptional
coactivator that associates with a member of the general transcription fact
or TFIID.