BIOMAT Database Logo BIOMAT Database Logo

Characterization of the transcriptional regulator YY1. The bipartite transactivation domain is independent of interaction with the TATA box-binding protein, transcription factor IIB, TAFII55, or cAMP-responsive element-binding protein (CPB)-binding protein. 1997

M Austen, and B Lüscher, and J M Lüscher-Firzlaff
Institut für Molekularbiologie, Medizinische Hochschule Hannover, Carl-Neuberg-Strasse 1, 30623 Hannover, Federal Republic of Germany.

YY1 is a multifunctional transcription factor implicated in both positive and negative regulation of gene expression as well as in initiation of transcription. We show that YY1 is ubiquitously expressed in growing, differentiated, and growth-arrested cells. The protein is phosphorylated and has a half-life of 3.5 h. To define functional domains, we have generated a large panel of YY1 mutant proteins. These were used to define precisely the DNA-binding domain, the region responsible for nuclear localization, and the transactivation domain. The two acidic domains at the N terminus each provide about half of the transcriptional activating activity. Furthermore, the spacer region between the Gly/Ala-rich and zinc finger domains has accessory function in transactivation. YY1 has been shown previously to bind to TAFII55, TATA box-binding protein, transcription factor IIB, and p300. In addition, we identified cAMP-responsive element-binding protein (CBP)-binding protein as a YY1 binding partner. Surprisingly, these proteins did not bind to the domains involved in transactivation, but rather to the zinc finger and Gly/Ala-rich domains of YY1. Thus, these proteins do not explain the transcriptional activating activity of YY1, but rather may be involved in repression or in initiation.

UI MeSH Term Description Entries
D011485 Protein Binding The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. Plasma Protein Binding Capacity,Binding, Protein
D011817 Rabbits A burrowing plant-eating mammal with hind limbs that are longer than its fore limbs. It belongs to the family Leporidae of the order Lagomorpha, and in contrast to hares, possesses 22 instead of 24 pairs of chromosomes. Belgian Hare,New Zealand Rabbit,New Zealand Rabbits,New Zealand White Rabbit,Rabbit,Rabbit, Domestic,Chinchilla Rabbits,NZW Rabbits,New Zealand White Rabbits,Oryctolagus cuniculus,Chinchilla Rabbit,Domestic Rabbit,Domestic Rabbits,Hare, Belgian,NZW Rabbit,Rabbit, Chinchilla,Rabbit, NZW,Rabbit, New Zealand,Rabbits, Chinchilla,Rabbits, Domestic,Rabbits, NZW,Rabbits, New Zealand,Zealand Rabbit, New,Zealand Rabbits, New,cuniculus, Oryctolagus
D002373 Cyclic AMP Receptor Protein A transcriptional regulator in prokaryotes which, when activated by binding cyclic AMP, acts at several promoters. Cyclic AMP receptor protein was originally identified as a catabolite gene activator protein. It was subsequently shown to regulate several functions unrelated to catabolism, and to be both a negative and a positive regulator of transcription. Cell surface cyclic AMP receptors are not included (CYCLIC AMP RECEPTORS), nor are the eukaryotic cytoplasmic cyclic AMP receptor proteins, which are the regulatory subunits of CYCLIC AMP-DEPENDENT PROTEIN KINASES. Catabolic Gene Activators,Catabolite Activator Protein,Catabolite Gene Activator Protein,Catabolite Gene Activator Proteins,Activator Protein, Catabolite,Activator Proteins, Catabolite,Activator, Catabolic Gene,Activators, Catabolic Gene,Catabolic Gene Activator,Catabolite Activator Proteins,Catabolite Regulator Protein,Catabolite Regulator Proteins,Cyclic AMP Receptor Proteins,Gene Activator, Catabolic,Gene Activators, Catabolic,Protein, Catabolite Activator,Protein, Catabolite Regulator,Proteins, Catabolite Activator,Proteins, Catabolite Regulator,Regulator Protein, Catabolite,Regulator Proteins, Catabolite,cAMP Receptor Protein,cAMP Receptor Proteins,Protein, cAMP Receptor,Proteins, cAMP Receptor,Receptor Protein, cAMP,Receptor Proteins, cAMP
D004268 DNA-Binding Proteins Proteins which bind to DNA. The family includes proteins which bind to both double- and single-stranded DNA and also includes specific DNA binding proteins in serum which can be used as markers for malignant diseases. DNA Helix Destabilizing Proteins,DNA-Binding Protein,Single-Stranded DNA Binding Proteins,DNA Binding Protein,DNA Single-Stranded Binding Protein,SS DNA BP,Single-Stranded DNA-Binding Protein,Binding Protein, DNA,DNA Binding Proteins,DNA Single Stranded Binding Protein,DNA-Binding Protein, Single-Stranded,Protein, DNA-Binding,Single Stranded DNA Binding Protein,Single Stranded DNA Binding Proteins
D006367 HeLa Cells The first continuously cultured human malignant CELL LINE, derived from the cervical carcinoma of Henrietta Lacks. These cells are used for, among other things, VIRUS CULTIVATION and PRECLINICAL DRUG EVALUATION assays. Cell, HeLa,Cells, HeLa,HeLa Cell
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D014157 Transcription Factors Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process. Transcription Factor,Factor, Transcription,Factors, Transcription
D014158 Transcription, Genetic The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION. Genetic Transcription
D015534 Trans-Activators Diffusible gene products that act on homologous or heterologous molecules of viral or cellular DNA to regulate the expression of proteins. Nuclear Trans-Acting Factor,Trans-Acting Factors,Trans-Acting Factor,Trans-Activator,Transactivator,Transactivators,Factor, Nuclear Trans-Acting,Factor, Trans-Acting,Factors, Trans-Acting,Nuclear Trans Acting Factor,Trans Acting Factor,Trans Acting Factors,Trans Activator,Trans Activators,Trans-Acting Factor, Nuclear

Related Publications

M Austen, and B Lüscher, and J M Lüscher-Firzlaff
Interaction of the COOH-terminal transactivation domain of p65 NF-kappa B with TATA-binding protein, transcription factor IIB, and coactivators.
March 1995, The Journal of biological chemistry,
M Austen, and B Lüscher, and J M Lüscher-Firzlaff
High affinity interaction of yeast transcriptional regulator, Mot1, with TATA box-binding protein (TBP).
April 2001, The Journal of biological chemistry,
M Austen, and B Lüscher, and J M Lüscher-Firzlaff
YY1 is a negative regulator of transcription of three sterol regulatory element-binding protein-responsive genes.
May 1999, The Journal of biological chemistry,
M Austen, and B Lüscher, and J M Lüscher-Firzlaff
Characterization of human activating transcription factor 4, a transcriptional activator that interacts with multiple domains of cAMP-responsive element-binding protein (CREB)-binding protein.
September 1997, The Journal of biological chemistry,
M Austen, and B Lüscher, and J M Lüscher-Firzlaff
Structure of the genes encoding transcription factor IIB and TATA box-binding protein from Drosophila melanogaster.
February 1995, Gene,
M Austen, and B Lüscher, and J M Lüscher-Firzlaff
A bipartite DNA binding domain composed of direct repeats in the TATA box binding factor TFIID.
April 1992, Proceedings of the National Academy of Sciences of the United States of America,
M Austen, and B Lüscher, and J M Lüscher-Firzlaff
Direct interaction between the transcriptional activation domain of human p53 and the TATA box-binding protein.
February 1993, The Journal of biological chemistry,
M Austen, and B Lüscher, and J M Lüscher-Firzlaff
Direct interaction between adenovirus E1A protein and the TATA box binding transcription factor IID.
June 1991, Proceedings of the National Academy of Sciences of the United States of America,
M Austen, and B Lüscher, and J M Lüscher-Firzlaff
The minimal transactivation domain of the basic motif-leucine zipper transcription factor NRL interacts with TATA-binding protein.
November 2004, The Journal of biological chemistry,
M Austen, and B Lüscher, and J M Lüscher-Firzlaff
Transactivation ability of p53 transcriptional activation domain is directly related to the binding affinity to TATA-binding protein.
October 1995, The Journal of biological chemistry,
Copied contents to your clipboard!