PMID- 10744685
OWN - NLM
STAT- MEDLINE
DCOM- 20000508
LR  - 20210209
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 275
IP  - 14
DP  - 2000 Apr 7
TI  - The human transcription factor IID subunit human TATA-binding protein-associated 
      factor 28 interacts in a ligand-reversible manner with the vitamin D(3) and 
      thyroid hormone receptors.
PG  - 10064-71
AB  - Using coexpression in COS cells, we have identified novel interactions between 
      the human TATA-binding protein-associated factor 28 (hTAF(II)28) component of 
      transcription factor IID and the ligand binding domains (LBDs) of the nuclear 
      receptors for vitamin D3 (VDR) and thyroid hormone (TRalpha). Interaction between 
      hTAF(II)28 and the VDR and TR LBDs was ligand-reversible, whereas no interactions 
      between hTAF(II)28 and the retinoid X receptors (RXRs) or other receptors were 
      observed. TAF(II)28 interacted with two regions of the VDR, a 40-amino acid 
      region spanning alpha-helices H3-H5 and alpha-helix H8. Interactions were also 
      observed with the H3-H5 region of the TRalpha but not with the equivalent highly 
      related region of the RXRgamma. Fine mapping using RXR derivatives in which 
      single amino acids of the RXRgamma LBD have been replaced with their VDR 
      counterparts shows that the determinants for interaction with hTAF(II)28 are 
      located in alpha-helix H3 and are not identical to those previously identified 
      for interactions with hTAF(II)55. We also describe a mutation in the H3-H5 region 
      of the VDR LBD, which abolishes transactivation, and we show that interaction of 
      hTAF(II)28 with this mutant is no longer ligand-reversible.
FAU - Mengus, G
AU  - Mengus G
AD  - Institut de Genetique et de Biologie Moleculaire et Cellulaire, CNRS, INSERM, 
      Universite Louis Pasteur, BP-163-67404 Illkirch Cedex, France.
FAU - Gangloff, Y G
AU  - Gangloff YG
FAU - Carre, L
AU  - Carre L
FAU - Lavigne, A C
AU  - Lavigne AC
FAU - Davidson, I
AU  - Davidson I
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Ligands)
RN  - 0 (Receptors, Calcitriol)
RN  - 0 (Receptors, Retinoic Acid)
RN  - 0 (Receptors, Thyroid Hormone)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (Recombinant Proteins)
RN  - 0 (Retinoid X Receptors)
RN  - 0 (TAF11 protein, human)
RN  - 0 (TATA-Binding Protein Associated Factors)
RN  - 0 (Transcription Factor TFIID)
RN  - 0 (Transcription Factors)
RN  - 0 (Transcription Factors, TFII)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Binding Sites
MH  - COS Cells
MH  - DNA-Binding Proteins/*metabolism
MH  - Humans
MH  - Kinetics
MH  - Ligands
MH  - Molecular Sequence Data
MH  - Protein Structure, Secondary
MH  - Receptors, Calcitriol/*chemistry/*metabolism
MH  - Receptors, Retinoic Acid/metabolism
MH  - Receptors, Thyroid Hormone/*metabolism
MH  - Recombinant Fusion Proteins/chemistry/metabolism
MH  - Recombinant Proteins/metabolism
MH  - Retinoid X Receptors
MH  - Sequence Alignment
MH  - Sequence Homology, Amino Acid
MH  - *TATA-Binding Protein Associated Factors
MH  - Transcription Factor TFIID
MH  - Transcription Factors/*metabolism
MH  - Transcription Factors, TFII/*metabolism
MH  - Transfection
EDAT- 2000/04/01 09:00
MHDA- 2000/05/16 09:00
CRDT- 2000/04/01 09:00
PHST- 2000/04/01 09:00 [pubmed]
PHST- 2000/05/16 09:00 [medline]
PHST- 2000/04/01 09:00 [entrez]
AID - S0021-9258(19)89880-0 [pii]
AID - 10.1074/jbc.275.14.10064 [doi]
PST - ppublish
SO  - J Biol Chem. 2000 Apr 7;275(14):10064-71. doi: 10.1074/jbc.275.14.10064.