Requirement for TFIIH kinase activity in transcription by RNA polymerase II (Q28289887)

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author name string

S Akoulitchev

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T P Mäkelä

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D Reinberg

Functional redundancy and structural polymorphism in the large subunit of RNA polymerase II.

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language of work or name

English

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publication date

12 October 1995

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published in

Nature

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volume

377

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issue

6549

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page(s)

557-60

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cites work

1 reference

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The C-terminal domain of the largest subunit of RNA polymerase II of Saccharomyces cerevisiae, Drosophila melanogaster, and mammals: a conserved structure with an essential function

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Genetic analysis of the repetitive carboxyl-terminal domain of the largest subunit of mouse RNA polymerase II

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The nonphosphorylated form of RNA polymerase II preferentially associates with the preinitiation complex

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Phosphorylation of RNA polymerase II C-terminal domain and transcriptional elongation

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Mutations in RNA polymerase II enhance or suppress mutations in GAL4.

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RNA polymerase II C-terminal repeat influences response to transcriptional enhancer signals

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RNA polymerase II C-terminal domain required for enhancer-driven transcription

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An RNA polymerase II holoenzyme responsive to activators

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A multiprotein mediator of transcriptional activation and its interaction with the C-terminal repeat domain of RNA polymerase II.

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Phosphorylation of C-terminal domain of RNA polymerase II is not required in basal transcription

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The HIP1 initiator element plays a role in determining the in vitro requirement of the dihydrofolate reductase gene promoter for the C-terminal domain of RNA polymerase II.

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The MO15 cell cycle kinase is associated with the TFIIH transcription-DNA repair factor

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Association of Cdk-activating kinase subunits with transcription factor TFIIH

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Cdk-activating kinase complex is a component of human transcription factor TFIIH

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Transcription factors IIE and IIH and ATP hydrolysis direct promoter clearance by RNA polymerase II

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Mechanism and control of transcription initiation in prokaryotes

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Human general transcription factor IIH phosphorylates the C-terminal domain of RNA polymerase II

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The multifunctional TFIIH complex and transcriptional control

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A kinase-deficient transcription factor TFIIH is functional in basal and activated transcription

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Dual role of TFIIH in DNA excision repair and in transcription by RNA polymerase II

1 reference

7 January 2021