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Peter E. Shaw - One of the best experts on this subject based on the ideXlab platform.

  • activation of Ternary Complex factor elk 1 by stress activated protein kinases
    Current Biology, 1995
    Co-Authors: Hendrik Gille, Thomas Strahl, Peter E. Shaw
    Abstract:

    Abstract Background: The mammalian response to stress results in the activation of stress-activated protein kinases (also known as cJun N-terminal kinases; SAPKs or JNKs), which are a sub-group of the mitogen-activated protein (MAP) kinase family. The SAPKs are involved in the upregulation of activity of the transcription factor AP-1 by post-translational modification of two of its components, cJun and ATF2. AP-1 activity can also be elevated by increased expression of the Fos protein, a further AP-1 component. Elk-1 (also called p62 TCF ), a transcription factor involved in the induction of the expression from the c- fos promoter through the promoter's serum response element, is known to be activated as a result of phosphorylation by the MAP kinases ERK1 and ERK2. However, induction of c- fos expression in response to noxious agents takes place in the absence of ERK activation. We therefore investigated whether SAPKs similarly upregulate c- fos expression by phosphorylating Elk-1. Results Elk-1 is activated in response to stimuli other than mitogenic signals. Both p46 SAPK and p54 SAPK interact physically with, and phosphorylate, Elk-1. The capacity of Elk-1 to form a Ternary Complex with serum response factor in vitro is thereby elevated. In vivo, selective activation of SAPKs stimulates formation of the Ternary Complex containing Elk-1, serum response factor and the serum response element, and enhances Elk-1-dependent transcription. Expression of the SAPK upstream-activator kinase, MEKK1, induces SAPK activation and c- fos transcription in the absence of ERK activity. Phosphopeptide mapping of Elk-1 phosphorylated with p46 SAPK or p54 SAPK reveals Ser383, a residue critical for Ternary Complex formation and transcriptional activation, to be the major phosphorylation site. Conclusion Elk-1 responds to stress-induced, as well as mitogenic, signals by stimulating c- fos transcription through the serum response element. Phosphorylation of Elk-1 by SAPKs and the ensuing expression of Fos protein thus constitutes an additional mechanism by which cells can upregulate AP-1 activity in response to stress.

  • ERK phosphorylation potentiates Elk-1-mediated Ternary Complex formation and transactivation.
    The EMBO journal, 1995
    Co-Authors: Hendrik Gille, Kortenjann M, O. Thomae, C. Moomaw, Clive A. Slaughter, Melanie H. Cobb, Peter E. Shaw
    Abstract:

    Induction of the human c-fos proto-oncogene by mitogens depends on the formation of a Ternary Complex by p62TCF with the serum response factor (SRF) and the serum response element (SRE). We demonstrate that Elk-1, a protein closely related to p62TCF in function, is a nuclear target of two members of the MAP kinase family, ERK1 and ERK2. Phosphorylation of Elk-1 increases the yield of Ternary Complex in vitro. At least five residues in the C-terminal domain of Elk-1 are phosphorylated upon growth factor stimulation of NIH3T3 cells. These residues are also phosphorylated by purified ERK1 in vitro, as determined by a combination of phosphopeptide sequencing and 2-D peptide mapping. Conversion of two of these phospho-acceptor sites to alanine impairs the formation of Ternary Complexes by the resulting Elk-1 proteins. Removal of these serine residues also drastically diminishes activation of the c-fos promoter in epidermal growth factor-treated cells. Analogous mutations at other sites impair activation to a lesser extent without affecting Ternary Complex formation in vitro. Our results indicate that phosphorylation regulates Ternary Complex formation by Elk-1, which is a prerequisite for the manifestation of its transactivation potential at the c-fos SRE.

  • phosphorylation of transcription factor p62tcf by map kinase stimulates Ternary Complex formation at c fos promoter
    Nature, 1992
    Co-Authors: Hendrik Gille, Andrew D Sharrocks, Peter E. Shaw
    Abstract:

    Transcription of the proto-oncogene c-fos is stimulated rapidly and transiently by serum growth factors and mitogens. Critical for this response is the serum-response element which is bound in vivo in a Ternary Complex containing the transcription factors p67SRF and p62TCF (ref. 2). Disruption of the Ternary Complex correlates with impaired induction by serum and phorbol ester. Mitogen-activated protein (MAP) kinase is a serine/threonine kinase which is activated 1-5 minutes after treatment of cells with mitogens and growth factors that induce re-entry into the cell cycle, making MAP kinase a candidate for the transmission of proliferative signals. Here we show that p62TCF is phosphorylated by MAP kinase in vitro and that phosphorylation results in enhanced Ternary Complex formation. Serum-starved Swiss 3T3 cells treated with epidermal growth factor, which induces MAP kinase in these cells, are induced to express c-fos and yield p62TCF active in Ternary Complex formation. In contrast, treatment of Swiss 3T3 cells with insulin, which does not activate MAP kinase under these conditions, does not lead to enhanced Ternary Complex formation nor does it induce c-fos transcription. Our results link the expression of the human c-fos proto-oncogene to signal transduction pathways known to be activated before its own induction.

Robert G. Roeder - One of the best experts on this subject based on the ideXlab platform.

  • Crystal structure of a TFIIB–TBP–TATA-element Ternary Complex
    Nature, 1995
    Co-Authors: Dimitar B. Nikolov, Hua Chen, E.d. Halay, Anny Usheva, Koji Hisatake, Dong Kun Lee, Robert G. Roeder, Stephen K. Burley
    Abstract:

    The crystal structure of the transcription factorIIB (TFIIB)/TATA box-binding protein (TBP)/ TATA-element Ternary Complex is described at 2.7 A resolution. Core TFIIB resembles cyclin A, and recognizes the preformed TBP–DNA Complex through protein–protein and protein–DNA interactions. The amino-terminal domain of core TFIIB forms the downstream surface of the Ternary Complex, where it could fix the transcription start site. The remaining surfaces of TBP and the TFIIB can interact with TBP-associated factors, other class II initiation factors, and transcriptional activators and coactivators.

  • crystal structure of a tfiib tbp tata element Ternary Complex
    Nature, 1995
    Co-Authors: Dimitar B. Nikolov, Hua Chen, E.d. Halay, Anny Usheva, Koji Hisatake, Dong Kun Lee, Robert G. Roeder
    Abstract:

    The crystal structure of the transcription factorIIB (TFIIB)/TATA box-binding protein (TBP)/ TATA-element Ternary Complex is described at 2.7 A resolution. Core TFIIB resembles cyclin A, and recognizes the preformed TBP–DNA Complex through protein–protein and protein–DNA interactions. The amino-terminal domain of core TFIIB forms the downstream surface of the Ternary Complex, where it could fix the transcription start site. The remaining surfaces of TBP and the TFIIB can interact with TBP-associated factors, other class II initiation factors, and transcriptional activators and coactivators.

E.d. Halay - One of the best experts on this subject based on the ideXlab platform.

  • Crystal structure of a TFIIB–TBP–TATA-element Ternary Complex
    Nature, 1995
    Co-Authors: Dimitar B. Nikolov, Hua Chen, E.d. Halay, Anny Usheva, Koji Hisatake, Dong Kun Lee, Robert G. Roeder, Stephen K. Burley
    Abstract:

    The crystal structure of the transcription factorIIB (TFIIB)/TATA box-binding protein (TBP)/ TATA-element Ternary Complex is described at 2.7 A resolution. Core TFIIB resembles cyclin A, and recognizes the preformed TBP–DNA Complex through protein–protein and protein–DNA interactions. The amino-terminal domain of core TFIIB forms the downstream surface of the Ternary Complex, where it could fix the transcription start site. The remaining surfaces of TBP and the TFIIB can interact with TBP-associated factors, other class II initiation factors, and transcriptional activators and coactivators.

  • crystal structure of a tfiib tbp tata element Ternary Complex
    Nature, 1995
    Co-Authors: Dimitar B. Nikolov, Hua Chen, E.d. Halay, Anny Usheva, Koji Hisatake, Dong Kun Lee, Robert G. Roeder
    Abstract:

    The crystal structure of the transcription factorIIB (TFIIB)/TATA box-binding protein (TBP)/ TATA-element Ternary Complex is described at 2.7 A resolution. Core TFIIB resembles cyclin A, and recognizes the preformed TBP–DNA Complex through protein–protein and protein–DNA interactions. The amino-terminal domain of core TFIIB forms the downstream surface of the Ternary Complex, where it could fix the transcription start site. The remaining surfaces of TBP and the TFIIB can interact with TBP-associated factors, other class II initiation factors, and transcriptional activators and coactivators.

Hua Chen - One of the best experts on this subject based on the ideXlab platform.

  • Crystal structure of a TFIIB–TBP–TATA-element Ternary Complex
    Nature, 1995
    Co-Authors: Dimitar B. Nikolov, Hua Chen, E.d. Halay, Anny Usheva, Koji Hisatake, Dong Kun Lee, Robert G. Roeder, Stephen K. Burley
    Abstract:

    The crystal structure of the transcription factorIIB (TFIIB)/TATA box-binding protein (TBP)/ TATA-element Ternary Complex is described at 2.7 A resolution. Core TFIIB resembles cyclin A, and recognizes the preformed TBP–DNA Complex through protein–protein and protein–DNA interactions. The amino-terminal domain of core TFIIB forms the downstream surface of the Ternary Complex, where it could fix the transcription start site. The remaining surfaces of TBP and the TFIIB can interact with TBP-associated factors, other class II initiation factors, and transcriptional activators and coactivators.

  • crystal structure of a tfiib tbp tata element Ternary Complex
    Nature, 1995
    Co-Authors: Dimitar B. Nikolov, Hua Chen, E.d. Halay, Anny Usheva, Koji Hisatake, Dong Kun Lee, Robert G. Roeder
    Abstract:

    The crystal structure of the transcription factorIIB (TFIIB)/TATA box-binding protein (TBP)/ TATA-element Ternary Complex is described at 2.7 A resolution. Core TFIIB resembles cyclin A, and recognizes the preformed TBP–DNA Complex through protein–protein and protein–DNA interactions. The amino-terminal domain of core TFIIB forms the downstream surface of the Ternary Complex, where it could fix the transcription start site. The remaining surfaces of TBP and the TFIIB can interact with TBP-associated factors, other class II initiation factors, and transcriptional activators and coactivators.

Koji Hisatake - One of the best experts on this subject based on the ideXlab platform.

  • Crystal structure of a TFIIB–TBP–TATA-element Ternary Complex
    Nature, 1995
    Co-Authors: Dimitar B. Nikolov, Hua Chen, E.d. Halay, Anny Usheva, Koji Hisatake, Dong Kun Lee, Robert G. Roeder, Stephen K. Burley
    Abstract:

    The crystal structure of the transcription factorIIB (TFIIB)/TATA box-binding protein (TBP)/ TATA-element Ternary Complex is described at 2.7 A resolution. Core TFIIB resembles cyclin A, and recognizes the preformed TBP–DNA Complex through protein–protein and protein–DNA interactions. The amino-terminal domain of core TFIIB forms the downstream surface of the Ternary Complex, where it could fix the transcription start site. The remaining surfaces of TBP and the TFIIB can interact with TBP-associated factors, other class II initiation factors, and transcriptional activators and coactivators.

  • crystal structure of a tfiib tbp tata element Ternary Complex
    Nature, 1995
    Co-Authors: Dimitar B. Nikolov, Hua Chen, E.d. Halay, Anny Usheva, Koji Hisatake, Dong Kun Lee, Robert G. Roeder
    Abstract:

    The crystal structure of the transcription factorIIB (TFIIB)/TATA box-binding protein (TBP)/ TATA-element Ternary Complex is described at 2.7 A resolution. Core TFIIB resembles cyclin A, and recognizes the preformed TBP–DNA Complex through protein–protein and protein–DNA interactions. The amino-terminal domain of core TFIIB forms the downstream surface of the Ternary Complex, where it could fix the transcription start site. The remaining surfaces of TBP and the TFIIB can interact with TBP-associated factors, other class II initiation factors, and transcriptional activators and coactivators.