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Molecular and Cellular Biology, January 2001, p. 614-623, Vol. 21, No. 2
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.
0270-7306/01/$04.00+0 DOI: 10.1128/MCB.21.2.614-623.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Prodos Is a Conserved Transcriptional Regulator
That Interacts with dTAFII16 in Drosophila
melanogaster
*
Corresponding author. Mailing address: Instituto Cajal,
C.S.I.C., Ave. Dr. Arce 37, 28002 Madrid, Spain. Phone: 34 915854739. Fax: 34 915854754. E-mail: aferrus{at}cajal.csic.es.
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