scholarly journals Analysis of a hybrid TATA box binding protein originating from mesophilic and thermophilic donor organisms

2010 ◽  
Vol 24 (3-4) ◽  
pp. 233-237
Author(s):  
Annette Kopitz ◽  
Jörg Soppa ◽  
Karin Hauser
Keyword(s):  
Thermal Stability ◽  
Molecular Mechanisms ◽  
Binding Protein ◽  
Temperature Stability ◽  
Optimal Growth ◽  
Tata Box ◽  
High Sequence Identity ◽  
Methanosarcina Mazei ◽  
Methanothermobacter Thermoautotrophicus ◽  
Tata Box Binding Protein

The TATA Box Binding Protein (TBP) is a 20 kD protein that is essential and universally conserved in eucarya and archaea. Especially among archaea, organisms can be found that live below 0°C as well as organisms that grow above 100°C. The archaeal TBPs show a high sequence identity and a similar structure consisting of α-helices andβ-sheets that are arranged in a saddle-shape 2-symmetric fold. In previous studies, we have characterized the thermal stability of thermophilic and mesophilic archaeal TBPs by infrared spectroscopy and showed the correlation between the transition temperature (Tm) and the optimal growth temperature (OGT) of the respective donor organism. In this study, a “new” mutant TBP has been constructed, produced, purified and analyzed for a deeper understanding of the molecular mechanisms of thermoadaptation. Theβ-sheet part of the mutant consists of the TBP fromMethanothermobacter thermoautotrophicus(OGT 65°C, MtTBP65) whose α-helices have been exchanged by those ofMethanosarcina mazei(OGT 37°C, MmTBP37). The Hybrid-TBP irreversibly aggregates after thermal unfolding just like MmTBP37 and MtTBP65, but theTm lies between that of MmTBP37 and MtTBP65 indicating that the interaction between the α-helical andβ-sheet part of the TBP is crucial for the thermal stability. The temperature stability is probably encoded in the variable α-helices that interact with the highly conserved and DNA bindingβ-sheets.

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.

scholarly journals The Small Nuclear RNA-activating Protein 190 Myb DNA Binding Domain Stimulates TATA Box-binding Protein-TATA Box Recognition

2003 ◽  
Vol 278 (20) ◽  
pp. 18649-18657 ◽  
Author(s):  
Craig S. Hinkley ◽  
Heather A. Hirsch ◽  
Liping Gu ◽  
Brandon LaMere ◽  
R. William Henry
Keyword(s):  
Dna Binding ◽  
Binding Protein ◽  
Binding Domain ◽  
Tata Box ◽  
Dna Binding Domain ◽  
Small Nuclear Rna ◽  
Nuclear Rna ◽  
Tata Box Binding Protein

scholarly journals Entamoeba histolytica TATA-box binding protein binds to different TATA variants in vitro

FEBS Journal ◽  
2005 ◽  
Vol 272 (6) ◽  
pp. 1354-1366 ◽  
Author(s):  
Guadalupe De Dios-Bravo ◽  
Juan Pedro Luna-Arias ◽  
Ana María Riverón ◽  
José J Olivares-Trejo ◽  
César López-Camarillo ◽  
...  
Keyword(s):  
Entamoeba Histolytica ◽  
Binding Protein ◽  
Tata Box ◽  
Tata Box Binding Protein
Sign in / Sign up

Export Citation Format

Share Document