PMID- 10594036
OWN - NLM
STAT- MEDLINE
DCOM- 20000110
LR  - 20210526
IS  - 0270-7306 (Print)
IS  - 1098-5549 (Electronic)
IS  - 0270-7306 (Linking)
VI  - 20
IP  - 1
DP  - 2000 Jan
TI  - The human TFIID components TAF(II)135 and TAF(II)20 and the yeast SAGA components 
      ADA1 and TAF(II)68 heterodimerize to form histone-like pairs.
PG  - 340-51
AB  - It has been previously proposed that the transcription complexes TFIID and SAGA 
      comprise a histone octamer-like substructure formed from a heterotetramer of 
      H4-like human hTAF(II)80 (or its Drosophila melanogaster dTAF(II)60 and yeast 
      [Saccharomyces cerevisiae] yTAF(II)60 homologues) and H3-like hTAF(II)31 
      (dTAF(II)40 and yTAF(II)17) along with two homodimers of H2B-like hTAF(II)20 
      (dTAF(II)30alpha and yTAF(II)61/68). However, it has not been formally shown that 
      hTAF(II)20 heterodimerizes via its histone fold. By two-hybrid analysis with 
      yeast and biochemical characterization of complexes formed by coexpression in 
      Escherichia coli, we showed that hTAF(II)20 does not homodimerize but 
      heterodimerizes with hTAF(II)135. Heterodimerization requires the alpha2 and 
      alpha3 helices of the hTAF(II)20 histone fold and is abolished by mutations in 
      the hydrophobic face of the hTAF(II)20 alpha2 helix. Interaction with hTAF(II)20 
      requires a domain of hTAF(II)135 which shows sequence homology to H2A. This 
      domain also shows homology to the yeast SAGA component ADA1, and we show that 
      yADA1 heterodimerizes with the histone fold region of yTAF(II)61/68, the yeast 
      hTAF(II)20 homologue. These results are indicative of a histone fold type of 
      interaction between hTAF(II)20-hTAF(II)135 and yTAF(II)68-yADA1, which therefore 
      constitute novel histone-like pairs in the TFIID and SAGA complexes.
FAU - Gangloff, Y G
AU  - Gangloff YG
AD  - Institut de Genetique et de Biologie Moleculaire et Cellulaire, CNRS/INSERM/ULP, 
      Illkirch Cedex, C.U. de Strasbourg, France.
FAU - Werten, S
AU  - Werten S
FAU - Romier, C
AU  - Romier C
FAU - Carre, L
AU  - Carre L
FAU - Poch, O
AU  - Poch O
FAU - Moras, D
AU  - Moras D
FAU - Davidson, I
AU  - Davidson I
LA  - eng
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 (Adaptor Proteins, Signal Transducing)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Fungal Proteins)
RN  - 0 (HFI1 protein, S cerevisiae)
RN  - 0 (Histones)
RN  - 0 (Plant Proteins)
RN  - 0 (SAGA protein, Emericella nidulans)
RN  - 0 (Saccharomyces cerevisiae Proteins)
RN  - 0 (TAF2 protein, S cerevisiae)
RN  - 0 (TATA-Binding Protein Associated Factors)
RN  - 0 (Trans-Activators)
RN  - 0 (Transcription Factor TFIID)
RN  - 0 (Transcription Factors)
RN  - 0 (Transcription Factors, TFII)
SB  - IM
MH  - Adaptor Proteins, Signal Transducing
MH  - Amino Acid Sequence
MH  - DNA-Binding Proteins/chemistry/genetics
MH  - Dimerization
MH  - Fungal Proteins/chemistry/*genetics
MH  - Histones/chemistry/*genetics
MH  - Humans
MH  - Molecular Sequence Data
MH  - Plant Proteins/chemistry/*genetics
MH  - Protein Binding
MH  - Saccharomyces cerevisiae
MH  - *Saccharomyces cerevisiae Proteins
MH  - Sequence Alignment
MH  - *TATA-Binding Protein Associated Factors
MH  - *Trans-Activators
MH  - Transcription Factor TFIID
MH  - Transcription Factors/chemistry/genetics
MH  - Transcription Factors, TFII/chemistry/*genetics
PMC - PMC85089
EDAT- 1999/12/14 00:00
MHDA- 1999/12/14 00:01
CRDT- 1999/12/14 00:00
PHST- 1999/12/14 00:00 [pubmed]
PHST- 1999/12/14 00:01 [medline]
PHST- 1999/12/14 00:00 [entrez]
AID - 1179 [pii]
AID - 10.1128/MCB.20.1.340-351.2000 [doi]
PST - ppublish
SO  - Mol Cell Biol. 2000 Jan;20(1):340-51. doi: 10.1128/MCB.20.1.340-351.2000.