scholarly journals Initiation of zebrafish haematopoiesis by the TATA-box-binding protein-related factor Trf3

Nature ◽  
2007 ◽  
Vol 450 (7172) ◽  
pp. 1082-1085 ◽  
Author(s):  
Daniel O. Hart ◽  
Tamal Raha ◽  
Nathan D. Lawson ◽  
Michael R. Green
Keyword(s):  
Binding Protein ◽  
Tata Box ◽  
Related Factor ◽  
Tata Box Binding Protein

scholarly journals TRF3, a TATA-box-binding protein-related factor, is vertebrate-specific and widely expressed

2003 ◽  
Vol 100 (25) ◽  
pp. 14887-14891 ◽  
Author(s):  
S. P. Persengiev ◽  
X. Zhu ◽  
B. L. Dixit ◽  
G. A. Maston ◽  
E. L. W. Kittler ◽  
...  
Keyword(s):  
Binding Protein ◽  
Tata Box ◽  
Related Factor ◽  
Tata Box Binding Protein

scholarly journals Differential Utilization of TATA Box-binding Protein (TBP) and TBP-related Factor 1 (TRF1) at Different Classes of RNA Polymerase III Promoters

2013 ◽  
Vol 288 (38) ◽  
pp. 27564-27570 ◽  
Author(s):  
Neha Verma ◽  
Ko-Hsuan Hung ◽  
Jin Joo Kang ◽  
Nermeen H. Barakat ◽  
William E. Stumph
Keyword(s):  
Rna Polymerase ◽  
Binding Protein ◽  
Rna Polymerase Iii ◽  
Tata Box ◽  
Related Factor ◽  
U6 Snrna ◽  
Polymerase Iii ◽  
Tata Box Binding Protein ◽  
In Cells

In the fruit fly Drosophila melanogaster, RNA polymerase III transcription was found to be dependent not upon the canonical TATA box-binding protein (TBP) but instead upon the TBP-related factor 1 (TRF1) (Takada, S., Lis, J. T., Zhou, S., and Tjian, R. (2000) Cell 101, 459–469). Here we confirm that transcription of fly tRNA genes requires TRF1. However, we unexpectedly find that U6 snRNA gene promoters are occupied primarily by TBP in cells and that knockdown of TBP, but not TRF1, inhibits U6 transcription in cells. Moreover, U6 transcription in vitro effectively utilizes TBP, whereas TBP cannot substitute for TRF1 to promote tRNA transcription in vitro. Thus, in fruit flies, different classes of RNA polymerase III promoters differentially utilize TBP and TRF1 for the initiation of transcription.

scholarly journals Polymerase (Pol) III TATA Box-Binding Protein (TBP)-Associated Factor Brf Binds to a Surface on TBP Also Required for Activated Pol II Transcription

1998 ◽  
Vol 18 (3) ◽  
pp. 1692-1700 ◽  
Author(s):  
Yuhong Shen ◽  
George A. Kassavetis ◽  
Gene O. Bryant ◽  
Arnold J. Berk
Keyword(s):  
Gene Transcription ◽  
Transcription Initiation ◽  
Binding Protein ◽  
Tata Box ◽  
Related Factor ◽  
In Vitro Synthesis ◽  
Pol Ii ◽  
U6 Snrna ◽  
Tata Box Binding Protein ◽  
Pol Iii

ABSTRACT The TATA box-binding protein (TBP) plays an essential role in transcription by all three eukaryotic nuclear RNA polymerases, polymerases (Pol) I, II, and III. In each case, TBP interacts with class-specific TBP-associated factors (TAFs) to form class-specific transcription initiation factors. For yeast Pol III transcription, TBP associates with Brf (from TFIIB-related factor) and B", two Pol III TAFs, to form Pol III transcription factor TFIIIB. Here, we identify TBP surface residues that are required for interaction with yeast Pol III TAFs. Ninety-one human TBP surface residue mutants with radical substitutions were analyzed for the ability to form stable gel shift complexes with purified Brf and B" and for their activities for in vitro synthesis of yeast U6 snRNA. Mutations in a large positively charged epitope extending from the top (that is, on the surface opposite the DNA-facing “saddle” of TBP) and onto the side of the first TBP repeat inhibited binding to Brf (residues K181, L185, R186, E206, R231, L232, R235, K236, R239, Q242, K243, K249, and F250). A triple-mutant TBP (R231E + R235E + R239S) had greatly reduced activity for yeast U6 snRNA gene transcription while remaining active for Pol II basal transcription. Similar results were observed when selected mutations were introduced into yeast TBP at equivalent positions. A C-terminal fragment of Brf lacking the region of homology with TFIIB retains the ability to bind TBP-DNA complexes (G. Kassavetis, C. Bardeleben, A. Kumar, E. Ramirez, and E. P. Geiduschek, Mol. Cell. Biol. 17:5299–5306, 1997); the same TBP mutations reduced binding by this fragment. Mutations in TBP residues that interact with TFIIB did not affect Brf binding or U6 gene transcription. These results indicate that Brf and TFIIB interact differently with TBP. An extensively overlapping epitope on the top surface of TBP was found previously to be required for activated Pol II transcription and has been hypothesized to interact with Pol II TAFs. Our results map the surface of TBP that interacts with Brf and suggest that Pol II and Pol III TAFs interact with the same surface of TBP.

scholarly journals TATA box-binding protein (TBP)-related factor 2 (TRF2), a third member of the TBP family

1999 ◽  
Vol 96 (9) ◽  
pp. 4791-4796 ◽  
Author(s):  
M. D. Rabenstein ◽  
S. Zhou ◽  
J. T. Lis ◽  
R. Tjian
Keyword(s):  
Binding Protein ◽  
Tata Box ◽  
Related Factor ◽  
Tata Box Binding Protein
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