scholarly journals Compensatory Change of Interacting Amino Acids in the Coevolution of Transcriptional Coactivator MBF1 and TATA-Box–Binding Protein

2007 ◽  
Vol 24 (7) ◽  
pp. 1458-1463 ◽  
Author(s):  
Qing-Xin Liu ◽  
Naomi Nakashima-Kamimura ◽  
Kazuho Ikeo ◽  
Susumu Hirose ◽  
Takashi Gojobori
Keyword(s):  
Amino Acids ◽  
Binding Protein ◽  
Tata Box ◽  
Transcriptional Coactivator ◽  
Compensatory Change ◽  
Tata Box Binding Protein

scholarly journals Translation in amino-acid-poor environments is limited by tRNAGln charging

eLife ◽  
2020 ◽  
Vol 9 ◽  
Author(s):  
Natalya N Pavlova ◽  
Bryan King ◽  
Rachel H Josselsohn ◽  
Sara Violante ◽  
Victoria L Macera ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Mammalian Cells ◽  
Tata Box ◽  
Transcriptional Coactivator ◽  
Core Binding Factor ◽  
Amino Acid Availability ◽  
Binding Factor ◽  
Tata Box Binding Protein ◽  
Extracellular Amino Acid

An inadequate supply of amino acids leads to accumulation of uncharged tRNAs, which can bind and activate GCN2 kinase to reduce translation. Here, we show that glutamine-specific tRNAs selectively become uncharged when extracellular amino acid availability is compromised. In contrast, all other tRNAs retain charging of their cognate amino acids in a manner that is dependent upon intact lysosomal function. In addition to GCN2 activation and reduced total translation, the reduced charging of tRNAGln in amino-acid-deprived cells also leads to specific depletion of proteins containing polyglutamine tracts including core-binding factor α1, mediator subunit 12, transcriptional coactivator CBP and TATA-box binding protein. Treating amino-acid-deprived cells with exogenous glutamine or glutaminase inhibitors restores tRNAGln charging and the levels of polyglutamine-containing proteins. Together, these results demonstrate that the activation of GCN2 and the translation of polyglutamine-encoding transcripts serve as key sensors of glutamine availability in mammalian cells.

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
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