Evidence map›Paper›PMID 26945063›Full record

ArticleThe Journal of biological chemistry2016

Biochemical Analysis of Yeast Suppressor of Ty 4/5 (Spt4/5) Reveals the Importance of Nucleic Acid Interactions in the Prevention of RNA Polymerase II Arrest.

J Brooks Crickard, Jianhua Fu, Joseph C Reese

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
5.4field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

44 citing papers in PubMed, 62 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. New roles for elongation factors in RNA polymerase II ubiquitylation and degradation.Biochimica et biophysica acta. Gene regulatory mechanisms · 2023
    Review
  11. Allosteric mechanism of transcription inhibition by NusG-dependent pausing of RNA polymerase.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. NusG controls transcription pausing and RNA polymerase translocation throughout theProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  18. Review
  19. The capping enzyme facilitates promoter escape and assembly of a follow-on preinitiation complex for reinitiation.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 1 country.

J Brooks CrickardFrom the Department of Biochemistry and Molecular Biology, Center for Eukaryotic Gene Regulation, Penn State University, University Park, Pennsylvania 16802 and.
Jianhua Futhe Department of Biochemistry, Medical College of Wisconsin, Milwaukee, Wisconsin 53226.
Joseph C ReeseFrom the Department of Biochemistry and Molecular Biology, Center for Eukaryotic Gene Regulation, Penn State University, University Park, Pennsylvania 16802 and Jcr8@psu.edu.
Pennsylvania State University · USMedical College of Wisconsin · US

Funding

REGULATION OF DNA DAMAGE INDUCED GENES BY YEAST TAFIISR01GM058672 · NIGMS · PENNSYLVANIA STATE UNIVERSITY-UNIV PARK · PI REESE, JOSEPH C · 1999 to 2019
$6.5M
Structural Mechanism of RNA Polymerase II Early ElongationR01GM100997 · NIGMS · MEDICAL COLLEGE OF WISCONSIN · PI FU, JIANHUA · 2012 to 2015
$1.2M
NIGMS NIH HHS R01 GM058672NIGMS NIH HHS R01 GM100997
6 · The paper itself

Abstract

RNA polymerase II (RNAPII) undergoes structural changes during the transitions from initiation, elongation, and termination, which are aided by a collection of proteins called elongation factors. NusG/Spt5 is the only elongation factor conserved in all domains of life. Although much information exists about the interactions between NusG/Spt5 and RNA polymerase in prokaryotes, little is known about how the binding of eukaryotic Spt4/5 affects the biochemical activities of RNAPII. We characterized the activities of Spt4/5 and interrogated the structural features of Spt5 required for it to interact with elongation complexes, bind nucleic acids, and promote transcription elongation. The eukaryotic specific regions of Spt5 containing the Kyrpides, Ouzounis, Woese domains are involved in stabilizing the association with the RNAPII elongation complex, which also requires the presence of the nascent transcript. Interestingly, we identify a region within the conserved NusG N-terminal (NGN) domain of Spt5 that contacts the non-template strand of DNA both upstream of RNAPII and in the transcription bubble. Mutating charged residues in this region of Spt5 did not prevent Spt4/5 binding to elongation complexes, but abrogated the cross-linking of Spt5 to DNA and the anti-arrest properties of Spt4/5, thus suggesting that contact between Spt5 (NGN) and DNA is required for Spt4/5 to promote elongation. We propose that the mechanism of how Spt5/NGN promotes elongation is fundamentally conserved; however, the eukaryotic specific regions of the protein evolved so that it can serve as a platform for other elongation factors and maintain its association with RNAPII as it navigates genomes packaged into chromatin.

Indexed as

Chromosomal Proteins, Non-HistoneNuclear ProteinsNucleic AcidsProtein BindingProtein ConformationRNA Polymerase IISaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscriptional Elongation FactorsTranscription, GeneticChromosomal Proteins, Non-HistoneNuclear ProteinsNucleic AcidsRNA Polymerase IISaccharomyces cerevisiae ProteinsSPT4 protein, S cerevisiaeSPT5 transcriptional elongation factorTranscriptional Elongation FactorsDNA Protein Interactionsgene transcriptionRNA polymerase IISpt4/5transcription elongation factortranscription factortranscription regulation

Identifiers

PMID26945063
PMCPMC4858988
OpenAlexW2288918732

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.