Evidence map›Paper›PMID 27044865›Full record

ArticleMolecular and cellular biology2016

Fine-Tuning of FACT by the Ubiquitin Proteasome System in Regulation of Transcriptional Elongation.

Rwik Sen, Jannatul Ferdoush, Amala Kaja, Sukesh R Bhaumik

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.2field-weighted citation impact, top 20% 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

17 citing papers in PubMed, 26 citations in OpenAlex.

  1. Review
  2. Facilitates Chromatin Transcription in Breast and Other Cancers.Advances in experimental medicine and biology · 2024
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Quality control of cytoplasmic proteins inside the nucleus.Computational and structural biotechnology journal · 2022
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Structure and function of the histone chaperone FACT - Resolving FACTual issues.Biochimica et biophysica acta. Gene regulatory mechanisms · 2018
    Review
  14. Article
  15. Article
  16. Article
  17. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Rwik SenDepartment of Biochemistry and Molecular Biology, Southern Illinois University School of Medicine, Carbondale, Illinois, USA.
Jannatul FerdoushDepartment of Biochemistry and Molecular Biology, Southern Illinois University School of Medicine, Carbondale, Illinois, USA.
Amala KajaDepartment of Biochemistry and Molecular Biology, Southern Illinois University School of Medicine, Carbondale, Illinois, USA.
Sukesh R BhaumikDepartment of Biochemistry and Molecular Biology, Southern Illinois University School of Medicine, Carbondale, Illinois, USA sbhaumik@siumed.edu.
Southern Illinois University School of Medicine · US

Funding

Ubiquitin-proteasome system regulation of a transcriptional co-activator, SAGA, and associated functionsR15GM088798 · NIGMS · SOUTHERN ILLINOIS UNIVERSITY CARBONDALE · PI BHAUMIK, SUKESH R. · 2009 to 2018
$997k
NIGMS NIH HHS R15 GM088798
6 · The paper itself

Abstract

FACT (facilitates chromatin transcription), an evolutionarily conserved histone chaperone involved in transcription and other DNA transactions, is upregulated in cancers, and its downregulation is associated with cellular death. However, it is not clearly understood how FACT is fine-tuned for normal cellular functions. Here, we show that the FACT subunit Spt16 is ubiquitylated by San1 (an E3 ubiquitin ligase) and degraded by the 26S proteasome. Enhanced abundance of Spt16 in the absence of San1 impairs transcriptional elongation. Likewise, decreased abundance of Spt16 also reduces transcription. Thus, an optimal level of Spt16 is required for efficient transcriptional elongation, which is maintained by San1 via ubiquitylation and proteasomal degradation. Consistently, San1 associates with the coding sequences of active genes to regulate Spt16's abundance. Further, we found that enhanced abundance of Spt16 in the absence of San1 impairs chromatin reassembly at the coding sequence, similarly to the results seen following inactivation of Spt16. Efficient chromatin reassembly enhances the fidelity of transcriptional elongation. Taken together, our results demonstrate for the first time a fine-tuning of FACT by a ubiquitin proteasome system in promoting chromatin reassembly in the wake of elongating RNA polymerase II and transcriptional elongation, thus revealing novel regulatory mechanisms of gene expression.

Indexed as

Chromatin Assembly and DisassemblyGene Expression Regulation, FungalProteasome Endopeptidase ComplexRNA, FungalSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscriptional Elongation FactorsTranscription Elongation, GeneticUbiquitinationUbiquitin-Protein LigasesATP dependent 26S proteaseProteasome Endopeptidase ComplexRNA, FungalSaccharomyces cerevisiae ProteinsSAN1 protein, S cerevisiaeSPT16 protein, S cerevisiaeTranscriptional Elongation FactorsUbiquitin-Protein Ligases

Identifiers

PMID27044865
PMCPMC4959319
OpenAlexW2337662543

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.