Human TAFII30 is present in a distinct TFIID complex and is required for transcriptional activation by the estrogen receptor (Q24321811)

identical protein binding

GOA release 2020-03-11

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GOA release 2020-03-11

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5

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Irwin Davidson

object named as

I Davidson

4

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László Tora

object named as

L Tora

6

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author name string

X Jacq

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C Brou

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Y Lutz

Unique TATA-binding protein-containing complexes and cofactors involved in transcription by RNA polymerases II and III

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publication date

7 October 1994

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language of work or name

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79

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issue

1

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page(s)

107-17

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cites work

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Cloning and expression of Drosophila TAFII60 and human TAFII70 reveal conserved interactions with other subunits of TFIID

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DNA sequence and comparative analyses of the equine herpesvirus type 1 immediate early gene

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Functional domains of the human estrogen receptor

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The estrogen receptor binds tightly to its responsive element as a ligand-induced homodimer

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Multiple and cooperative trans-activation domains of the human glucocorticoid receptor

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The human estrogen receptor has two independent nonacidic transcriptional activation functions

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Five intermediate complexes in transcription initiation by RNA polymerase II

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Distinct classes of transcriptional activating domains function by different mechanisms

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Cloning, expression, and transcriptional properties of the human enhancer factor TEF-1

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Purification, cloning, and RXR identity of the HeLa cell factor with which RAR or TR heterodimerizes to bind target sequences efficiently

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Drosophila TAFII40 interacts with both a VP16 activation domain and the basal transcription factor TFIIB.

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Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase

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A highly conserved region in the hormone-binding domain of the human estrogen receptor functions as an efficient transactivation domain in yeast

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7 January 2021

The complexities of eukaryotic transcription initiation: regulation of preinitiation complex assembly

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Expression in Escherichia coli: purification and properties of the yeast general transcription factor TFIID.

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Cloning of murine alpha and beta retinoic acid receptors and a novel receptor gamma predominantly expressed in skin

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Direct and selective binding of an acidic transcriptional activation domain to the TATA-box factor TFIID

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Evidence for interaction of different eukaryotic transcriptional activators with distinct cellular targets

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Cloning and expression of human TAFII250: a TBP-associated factor implicated in cell-cycle regulation

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The p250 subunit of native TATA box-binding factor TFIID is the cell-cycle regulatory protein CCG1.

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The dTAFII80 subunit of Drosophila TFIID contains beta-transducin repeats.

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Eukaryotic activators function during multiple steps of preinitiation complex assembly

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Identification of two transactivation domains in the mouse oestrogen receptor

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Different TBP-associated factors are required for mediating the stimulation of transcription in vitro by the acidic transactivator GAL-VP16 and the two nonacidic activation functions of the estrogen receptor.

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Sequence-specific transactivators counteract topoisomerase II-mediated inhibition of in vitro transcription by RNA polymerases I and II.

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The mammalian TFIID protein is present in two functionally distinct complexes

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Coactivators for a proline-rich activator purified from the multisubunit human TFIID complex

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The Zta trans-activator protein stabilizes TFIID association with promoter DNA by direct protein-protein interaction

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Holo-TFIID supports transcriptional stimulation by diverse activators and from a TATA-less promoter

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Molecular cloning and characterization of dTAFII30 alpha and dTAFII30 beta: two small subunits of Drosophila TFIID.

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Factors (TAFs) required for activated transcription interact with TATA box-binding protein conserved core domain.

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TBP, a universal eukaryotic transcription factor?

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General initiation factors for RNA polymerase II.

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