PMID- 10409738
OWN - NLM
STAT- MEDLINE
DCOM- 19990819
LR  - 20240407
IS  - 0270-7306 (Print)
IS  - 1098-5549 (Electronic)
IS  - 0270-7306 (Linking)
VI  - 19
IP  - 8
DP  - 1999 Aug
TI  - Human TAF(II)55 interacts with the vitamin D(3) and thyroid hormone receptors and 
      with derivatives of the retinoid X receptor that have altered transactivation 
      properties.
PG  - 5486-94
AB  - We have identified novel interactions between the human (h)TATA-binding 
      protein-associated factor TAF(II)55 and the ligand-binding domains (LBDs) of the 
      nuclear receptors for vitamin D(3) (VDR) and thyroid hormone (TRalpha). Following 
      expression in Cos cells, hTAF(II)55 interacts with the VDR and TRalpha LBDs in a 
      ligand-independent manner whereas no interactions with the retinoid X receptors 
      (RXRs) or with other receptors were observed. Deletion mapping indicates that 
      hTAF(II)55 interacts with a 40-amino-acid region spanning alpha-helices H3 to H5 
      of the VDR and TRalpha LBDs but not with the equivalent highly related region of 
      RXRgamma. TAF(II)55 also interacts with chimeric receptors in which the H3-to-H5 
      region of RXRgamma has been replaced with that of the VDR or TRalpha. 
      Furthermore, replacement of two single amino acids of the RXRgamma LBD with their 
      VDR counterparts allows the RXRgamma LBD to interact with hTAF(II)55 while the 
      corresponding double substitution allows a much stronger interaction. In 
      transfection experiments, the single mutated RXRgamma LBDs activate transcription 
      to fivefold higher levels than wild-type RXRgamma while the double mutation 
      activates transcription to a level comparable to that observed with the VDR. 
      There is therefore a correlation between the ability of the modified RXRs to 
      interact with hTAF(II)55 and transactivation. These results strongly suggest that 
      the TAF(II)55 interactions with the modified RXR LBDs modulate transcriptional 
      activation.
FAU - Lavigne, A C
AU  - Lavigne AC
AD  - Institut de Genetique et de Biologie Moleculaire et Cellulaire, CNRS/INSERM/ULP, 
      Illkirch Cedex, C.U. de Strasbourg, France.
FAU - Mengus, G
AU  - Mengus G
FAU - Gangloff, Y G
AU  - Gangloff YG
FAU - Wurtz, J M
AU  - Wurtz JM
FAU - Davidson, I
AU  - Davidson I
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Mol Cell Biol
JT  - Molecular and cellular biology
JID - 8109087
RN  - 0 (Ligands)
RN  - 0 (Macromolecular Substances)
RN  - 0 (Peptide Fragments)
RN  - 0 (Receptors, Calcitriol)
RN  - 0 (Receptors, Retinoic Acid)
RN  - 0 (Receptors, Thyroid Hormone)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (Retinoid X Receptors)
RN  - 0 (TAF7 protein, human)
RN  - 0 (TATA-Binding Protein Associated Factors)
RN  - 0 (Trans-Activators)
RN  - 0 (Transcription Factor TFIID)
RN  - 0 (Transcription Factors)
SB  - IM
MH  - Amino Acid Sequence
MH  - Amino Acid Substitution
MH  - Animals
MH  - Binding Sites
MH  - COS Cells
MH  - Chlorocebus aethiops
MH  - Humans
MH  - Ligands
MH  - Macromolecular Substances
MH  - Molecular Sequence Data
MH  - Mutagenesis, Site-Directed
MH  - Peptide Fragments/metabolism
MH  - Protein Binding
MH  - Receptors, Calcitriol/*metabolism
MH  - Receptors, Retinoic Acid/genetics/*metabolism
MH  - Receptors, Thyroid Hormone/*metabolism
MH  - Recombinant Fusion Proteins/metabolism
MH  - Retinoid X Receptors
MH  - Sequence Alignment
MH  - Sequence Deletion
MH  - Sequence Homology, Amino Acid
MH  - *TATA-Binding Protein Associated Factors
MH  - Trans-Activators/*metabolism
MH  - *Transcription Factor TFIID
MH  - Transcription Factors/genetics/*metabolism
MH  - *Transcriptional Activation
MH  - Transfection
PMC - PMC84390
EDAT- 1999/07/20 00:00
MHDA- 1999/07/20 00:01
PMCR- 1999/08/01
CRDT- 1999/07/20 00:00
PHST- 1999/07/20 00:00 [pubmed]
PHST- 1999/07/20 00:01 [medline]
PHST- 1999/07/20 00:00 [entrez]
PHST- 1999/08/01 00:00 [pmc-release]
AID - 1612 [pii]
AID - 10.1128/MCB.19.8.5486 [doi]
PST - ppublish
SO  - Mol Cell Biol. 1999 Aug;19(8):5486-94. doi: 10.1128/MCB.19.8.5486.