Newly Initiated RNA encounters a factor involved in splicing immediately upon emerging from within RNA polymerase II. (Q38336471)

2 September 2017

Newly Initiated RNA encounters a factor involved in splicing immediately upon emerging from within RNA polymerase II. (English)

1 reference

2 September 2017

Andrea Ujvári

1

1 reference

PubMed ID

15377657

2 September 2017

Donal S Luse

series ordinal

2

1 reference

PubMed ID

15377657

2 September 2017

language of work or name

English

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publication date

17 September 2004

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Journal of Biological Chemistry

2 September 2017

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2 September 2017

279

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2 September 2017

48

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2 September 2017

49773-49779

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Promoter escape by RNA polymerase II

2 September 2017

1 reference

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The RNA polymerase II elongation complex

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Transcription elongation by RNA polymerase II.

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Running with RNA polymerase: eukaryotic transcript elongation

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Integrating mRNA processing with transcription

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An extensive network of coupling among gene expression machines

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The link between mRNA processing and transcription: communication works both ways

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Complete, 12-subunit RNA polymerase II at 4.1-Å resolution: Implications for the initiation of transcription

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Structural basis of transcription: an RNA polymerase II elongation complex at 3.3 A resolution

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Structural basis of transcription: separation of RNA from DNA by RNA polymerase II

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Increased accommodation of nascent RNA in a product site on RNA polymerase II during arrest

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Promoter proximal sequences modulate RNA polymerase II elongation by a novel mechanism.

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Structural basis of transcription: RNA polymerase II at 2.8 angstrom resolution

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Dissociable Rpb4-Rpb7 subassembly of rna polymerase II binds to single-strand nucleic acid and mediates a post-recruitment step in transcription initiation.

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Structure of an archaeal homolog of the eukaryotic RNA polymerase II RPB4/RPB7 complex

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U2AF participates in the binding of TAP (NXF1) to mRNA

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Genome-wide analysis reveals an unexpected function for the Drosophila splicing factor U2AF50 in the nuclear export of intronless mRNAs.

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Structural changes in the RNA polymerase II transcription complex during transition from initiation to elongation

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The role of U2AF35 and U2AF65 in enhancer-dependent splicing

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Transcription on nucleosomal templates by RNA polymerase II in vitro: inhibition of elongation with enhancement of sequence-specific pausing.

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Characterization of a novel RNA polymerase II arrest site which lacks a weak 3' RNA-DNA hybrid

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A human RNA polymerase II-containing complex associated with factors necessary for spliceosome assembly

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Six human RNA polymerase subunits functionally substitute for their yeast counterparts

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Targeting of U2AF65 to sites of active splicing in the nucleus

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Cloning and domain structure of the mammalian splicing factor U2AF

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U2AF homology motifs: protein recognition in the RRM world

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Structuring of the 3' splice site by U2AF65.

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U2AF modulates poly(A) length control by the poly(A)-limiting element.

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RNA polymerase switches between inactivated and activated states By translocating back and forth along the DNA and the RNA.

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Combinatorial Control of Human RNA Polymerase II (RNAP II) Pausing and Transcript Cleavage by Transcription Factor IIF, Hepatitis δ Antigen, and Stimulatory Factor II

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Protein phosphatase-1 dephosphorylates the C-terminal domain of RNA polymerase-II

21 January 2018

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Stimulatory effect of splicing factors on transcriptional elongation

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21 January 2018

Identifiers

DOI

10.1074/JBC.M409087200

1 reference

2 September 2017

1 reference

PubMed ID

15377657