scholarly journals The Minimal Transactivation Domain of the Basic Motif-Leucine Zipper Transcription Factor NRL Interacts with TATA-binding Protein

2004 ◽  
Vol 279 (45) ◽  
pp. 47233-47241 ◽  
Author(s):  
James S. Friedman ◽  
Hemant Khanna ◽  
Prabodh K. Swain ◽  
Raphael DeNicola ◽  
Hong Cheng ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Leucine Zipper ◽  
Binding Protein ◽  
Tata Binding Protein ◽  
Transactivation Domain

scholarly journals Interaction of the COOH-terminal Transactivation Domain of p65 NF-κB with TATA-binding Protein, Transcription Factor IIB, and Coactivators

1995 ◽  
Vol 270 (13) ◽  
pp. 7219-7226 ◽  
Author(s):  
M. Lienhard Schmitz ◽  
Gertraud Stelzer ◽  
Herbert Altmann ◽  
Michael Meisterernst ◽  
Patrick A. Baeuerle
Keyword(s):  
Transcription Factor ◽  
Binding Protein ◽  
Tata Binding Protein ◽  
Transactivation Domain ◽  
Transcription Factor Iib ◽  
Protein Transcription

scholarly journals Molecular cloning of cellular genes encoding retinoblastoma-associated proteins: identification of a gene with properties of the transcription factor E2F.

1992 ◽  
Vol 12 (12) ◽  
pp. 5620-5631 ◽  
Author(s):  
B Shan ◽  
X Zhu ◽  
P L Chen ◽  
T Durfee ◽  
Y Yang ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Mammalian Cells ◽  
Leucine Zipper ◽  
T Antigen ◽  
Transactivation Domain ◽  
Recognition Sequence ◽  
Cellular Genes ◽  
Genes Encoding ◽  
Associated Proteins ◽  
Transcription Factor E2f

The retinoblastoma protein interacts with a number of cellular proteins to form complexes which are probably crucial for its normal physiological function. To identify these proteins, we isolated nine distinct clones by direct screening of cDNA expression libraries using purified RB protein as a probe. One of these clones, Ap12, is expressed predominantly at the G1-S boundary and in the S phase of the cell cycle. The nucleotide sequence of Ap12 has features characteristic of transcription factors. The C-terminal region binds to unphosphorylated RB in regions similar to those to which T antigen binds and contains a transactivation domain. A region containing a potential leucine zipper flanked by basic residues is able to bind an E2F recognition sequence specifically. Expression of Ap12 in mammalian cells significantly enhances E2F-dependent transcriptional activity. These results suggest that Ap12 encodes a protein with properties known to be characteristic of transcription factor E2F.

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