Eukaryotic transcription initiation machinery visualized at molecular level

Han, Yanping

doi:10.1080/21541264.2016.1237150

Cited by 8 publications

(5 citation statements)

References 40 publications

(80 reference statements)

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“…Engagement of upstream promoter DNA with general transcription factors is an essential step during transcription initiation. For Pol II, large conformational changes and species-specific features have been observed from the closed complex formation to active elongation ( Han and He, 2016 ; He et al, 2016 ; Plaschka et al, 2016 ). We have reported here cryo-EM structures of Pol I Initial Transcribing Complex captured in three different functional states ( Figure 4 ).…”

Section: Discussionmentioning

confidence: 99%

Structural mechanism of ATP-independent transcription initiation by RNA polymerase I

Han

Cheng

Nguyen

et al. 2017

eLife

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104

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Transcription initiation by RNA Polymerase I (Pol I) depends on the Core Factor (CF) complex to recognize the upstream promoter and assemble into a Pre-Initiation Complex (PIC). Here, we solve a structure of Saccharomyces cerevisiae Pol I-CF-DNA to 3.8 Å resolution using single-particle cryo-electron microscopy. The structure reveals a bipartite architecture of Core Factor and its recognition of the promoter from −27 to −16. Core Factor’s intrinsic mobility correlates well with different conformational states of the Pol I cleft, in addition to the stabilization of either Rrn7 N-terminal domain near Pol I wall or the tandem winged helix domain of A49 at a partially overlapping location. Comparison of the three states in this study with the Pol II system suggests that a ratchet motion of the Core Factor-DNA sub-complex at upstream facilitates promoter melting in an ATP-independent manner, distinct from a DNA translocase actively threading the downstream DNA in the Pol II PIC.DOI: http://dx.doi.org/10.7554/eLife.27414.001

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Section: Discussionmentioning

confidence: 99%

Structural mechanism of ATP-independent transcription initiation by RNA polymerase I

Han

Cheng

Nguyen

et al. 2017

eLife

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104

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“…In yeast, the ribosomal DNA (rDNA) is organized in approximately 200 tandem repeats on chromosome XII, of which about half are actively transcribed during exponential growth [ 3 ]. Transcription factors are universally important for control of transcription by all three Pols [ 3 , 4 , 5 , 6 , 7 ], and many factors have been identified to influence each step in transcription: initiation, elongation, and termination [ 8 , 9 , 10 ]. These factors play a variety of roles, including recruitment of the polymerase to the promoter region [ 11 , 12 , 13 ], organization of the DNA template [ 14 , 15 , 16 ], and binding to termination motifs and promoting release of the polymerase from the template [ 17 , 18 , 19 ].…”

Section: Introductionmentioning

confidence: 99%

Spt4 Promotes Pol I Processivity and Transcription Elongation

Huffines

Edwards

Schneider

2021

Genes

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RNA polymerases (Pols) I, II, and III collectively synthesize most of the RNA in a eukaryotic cell. Transcription by Pols I, II, and III is regulated by hundreds of trans-acting factors. One such protein, Spt4, has been previously identified as a transcription factor that influences both Pols I and II. Spt4 forms a complex with Spt5, described as the Spt4/5 complex (or DSIF in mammalian cells). This complex has been shown previously to directly interact with Pol I and potentially affect transcription elongation. The previous literature identified defects in transcription by Pol I when SPT4 was deleted, but the necessary tools to characterize the mechanism of this effect were not available at the time. Here, we use a technique called Native Elongating Transcript Sequencing (NET-seq) to probe for the global occupancy of Pol I in wild-type (WT) and spt4△ Saccharomyces cerevisiae (yeast) cells at single nucleotide resolution in vivo. Analysis of NET-seq data reveals that Spt4 promotes Pol I processivity and enhances transcription elongation through regions of the ribosomal DNA that are particularly G-rich. These data suggest that Spt4/5 may directly affect transcription elongation by Pol I in vivo.

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“…The entire initiation complex comprises approximately 70 polypeptides and has a molecular weight of around 4 MDa ( Table 1). The structural basis for Pol II initiation has been studied for over a decade, and progress has been reviewed recently [4][5][6][7].…”

Section: Introductionmentioning

confidence: 99%

Conserved RNA polymerase II initiation complex structure

Hantsche

Cramer

2017

Current Opinion in Structural Biology

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Recent cryo-electron microscopic studies have arrived at atomic models of the core transcription initiation complex comprising RNA polymerase (Pol) II and the basal transcription factors TBP, TFIIA, TFIIB, TFIIE, and TFIIF. A detailed comparison of two independently derived yeast and human core initiation complex structures reveals that they are virtually identical, demonstrating the conservation of the basic transcription machinery amongst eukaryotes. The additional factors TFIID, TFIIH, and Mediator have been located on the periphery of the core initiation complex, providing the topology of the entire initiation assembly, which comprises approximately 70 polypeptides with a molecular weight of 4 Megadalton. Address

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Eukaryotic transcription initiation machinery visualized at molecular level

Cited by 8 publications

References 40 publications

Structural mechanism of ATP-independent transcription initiation by RNA polymerase I

Structural mechanism of ATP-independent transcription initiation by RNA polymerase I

Spt4 Promotes Pol I Processivity and Transcription Elongation

Conserved RNA polymerase II initiation complex structure

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