scholarly journals Structures and implications of TBP–nucleosome complexes

2021 ◽  
Vol 118 (30) ◽  
pp. e2108859118
Author(s):  
Haibo Wang ◽  
Le Xiong ◽  
Patrick Cramer
Keyword(s):  
Electron Microscopy ◽  
Transcription Factors ◽  
Binding Protein ◽  
Tata Box ◽  
Gene Promoters ◽  
Preinitiation Complex ◽  
Histone Octamer ◽  
Cryo Electron Microscopy ◽  
Tata Box Binding Protein ◽  
Nucleosome Binding

The TATA box-binding protein (TBP) is highly conserved throughout eukaryotes and plays a central role in the assembly of the transcription preinitiation complex (PIC) at gene promoters. TBP binds and bends DNA, and directs adjacent binding of the transcription factors TFIIA and TFIIB for PIC assembly. Here, we show that yeast TBP can bind to a nucleosome containing the Widom-601 sequence and that TBP–nucleosome binding is stabilized by TFIIA. We determine three cryo-electron microscopy (cryo-EM) structures of TBP–nucleosome complexes, two of them containing also TFIIA. TBP can bind to superhelical location (SHL) –6, which contains a TATA-like sequence, but also to SHL +2, which is GC-rich. Whereas binding to SHL –6 can occur in the absence of TFIIA, binding to SHL +2 is only observed in the presence of TFIIA and goes along with detachment of upstream terminal DNA from the histone octamer. TBP–nucleosome complexes are sterically incompatible with PIC assembly, explaining why a promoter nucleosome generally impairs transcription and must be moved before initiation can occur.

Regulation of gene expression in the mouse oocyte and early preimplantation embryo: developmental changes in Sp1 and TATA box-binding protein, TBP

Development ◽  
1994 ◽  
Vol 120 (8) ◽  
pp. 2347-2357 ◽  
Author(s):  
D.M. Worrad ◽  
P.T. Ram ◽  
R.M. Schultz
Keyword(s):  
Gene Expression ◽  
Transcription Factors ◽  
Reporter Gene ◽  
Binding Protein ◽  
Tata Box ◽  
Oocyte Growth ◽  
Immunofluorescent Microscopy ◽  
Male Pronucleus ◽  
Female Pronucleus ◽  
Tata Box Binding Protein

We previously demonstrated that an Sp1-dependent reporter gene is preferentially expressed in G2 of the 1-cell mouse embryo following microinjection of the male pronucleus when compared to microinjection of the female pronucleus (P.T. Ram and R.M. Schultz, 1993, Dev. Biol. 156, 552–556). We also noted that expression of the reporter gene is not observed following microinjection of the germinal vesicle of the fully grown oocyte. In the present study, we examined expression of this reporter gene during oocyte growth, as well as the nuclear concentration of two transcription factors, Sp1 and the TATA box-binding protein, TBP, during oocyte growth and the first cell cycle. The extent of reporter gene expression decreases during oocyte growth and this decrease correlates with the decrease in nuclear concentration of Sp1, as determined by confocal immunofluorescent microscopy. In addition, results of immunoblotting experiments also indicate a similar decrease in the total concentration of Sp1 during oocyte growth. The nuclear concentration of TBP also decreases during oocyte growth, as determined by confocal immunofluorescent microscopy. Following fertilization, the pronuclear concentration of these two transcription factors increases in a time-dependent fashion and the concentration of each is greater in the male pronucleus as compared to the female pronucleus. For each pronucleus and for each transcription factor, this increase in nuclear concentration is inhibited by aphidicolin, which inhibits DNA synthesis. Last, the increase in nuclear concentration of these two proteins observed between the 1-cell and 2-cell stages does not require transcription or cytokinesis.

scholarly journals Ectopic expression of TATA box-binding protein induces shoot proliferation in Arabidopsis

FEBS Letters ◽  
2001 ◽  
Vol 489 (2-3) ◽  
pp. 187-191 ◽  
Author(s):  
You-Fang Li ◽  
Frédéric Dubois ◽  
Dao-Xiu Zhou
Keyword(s):  
Binding Protein ◽  
Ectopic Expression ◽  
Shoot Proliferation ◽  
Tata Box ◽  
Tata Box Binding Protein

scholarly journals Bidirectional binding of the TATA box binding protein to the TATA box

1997 ◽  
Vol 94 (25) ◽  
pp. 13475-13480 ◽  
Author(s):  
J. M. Cox ◽  
M. M. Hayward ◽  
J. F. Sanchez ◽  
L. D. Gegnas ◽  
S. van der Zee ◽  
...  
Keyword(s):  
Binding Protein ◽  
Tata Box ◽  
Tata Box Binding Protein

c-Fos-induced activation of a TATA-box-containing promoter involves direct contact with TATA-box-binding protein

1994 ◽  
Vol 14 (9) ◽  
pp. 6021-6029
Author(s):  
R Metz ◽  
A J Bannister ◽  
J A Sutherland ◽  
C Hagemeier ◽  
E C O'Rourke ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Transcriptional Activation ◽  
Binding Protein ◽  
Tata Box ◽  
Binding Motif ◽  
Protein Protein Interactions ◽  
High Concentrations ◽  
Tata Box Binding Protein

Transcriptional activation in eukaryotes involves protein-protein interactions between regulatory transcription factors and components of the basal transcription machinery. Here we show that c-Fos, but not a related protein, Fra-1, can bind the TATA-box-binding protein (TBP) both in vitro and in vivo and that c-Fos can also interact with the transcription factor IID complex. High-affinity binding to TBP requires c-Fos activation modules which cooperate to activate transcription. One of these activation modules contains a TBP-binding motif (TBM) which was identified through its homology to TBP-binding viral activators. This motif is required for transcriptional activation, as well as TBP binding. Domain swap experiments indicate that a domain containing the TBM can confer TBP binding on Fra-1 both in vitro and in vivo. In vivo activation experiments indicate that a GAL4-Fos fusion can activate a promoter bearing a GAL4 site linked to a TATA box but that this activity does not occur at high concentrations of GAL4-Fos. This inhibition (squelching) of c-Fos activity is relieved by the presence of excess TBP, indicating that TBP is a direct functional target of c-Fos. Removing the TBM from c-Fos severely abrogates activation of a promoter containing a TATA box but does not affect activation of a promoter driven only by an initiator element. Collectively, these results suggest that c-Fos is able to activate via two distinct mechanisms, only one of which requires contact with TBP. Since TBP binding is not exhibited by Fra-1, TBP-mediated activation may be one characteristic that discriminates the function of Fos-related proteins.

Sign in / Sign up

Export Citation Format

Share Document