Evidence map›Paper›PMID 35102600›Full record

ArticleThe EMBO journal2022

Spt5 histone binding activity preserves chromatin during transcription by RNA polymerase II.

Cecile Evrin, Albert Serra-Cardona, Shoufu Duan, Progya P Mukherjee, Zhiguo Zhang, Karim P M Labib

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.4field-weighted citation impact, top 10% 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

21 citing papers in PubMed, 31 citations in OpenAlex.

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  11. Toward structural understanding of eukaryotic transcription elongation.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2025
    Review
  12. Article
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  15. Article
  16. Review
  17. Review
  18. Structural advances in transcription elongation.Current opinion in structural biology · 2022
    Review
  19. 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

6 authors at 2 institutions in 2 countries.

Cecile Evrin *The MRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee, UK.
Albert Serra-Cardona *Institute for Cancer Genetics, Department of Pediatrics and Department of Genetics and Development, Columbia University Irving Medical Center, New York, NY, USA.
Shoufu DuanInstitute for Cancer Genetics, Department of Pediatrics and Department of Genetics and Development, Columbia University Irving Medical Center, New York, NY, USA.ORCID 0000-0003-0416-374X
Progya P MukherjeeThe MRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee, UK.
Zhiguo ZhangInstitute for Cancer Genetics, Department of Pediatrics and Department of Genetics and Development, Columbia University Irving Medical Center, New York, NY, USA.ORCID 0000-0002-9451-2685
Karim P M LabibThe MRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee, UK.ORCID 0000-0001-8861-379X
Cancer Genetics (United States) · USUniversity of Dundee · GB

Funding

Tumor Biology and Microenvironment ProgramP30CA013696 · NCI · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI Anil K Rustgi · 1985 to 2026
$115.3M
Mechanisms of Epigenetic inheritanceR35GM118015 · NIGMS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI Zhiguo Zhang · 2016 to 2026
$9.5M
Mechanisms for histone segregation at DNA replication forks and implications for epigenetic inheritance.K99GM134180 · NIGMS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI SERRA CARDONA, ALBERT · 2019 to 2020
$200k
Medical Research Council MC_UU_00018/4Medical Research Council MC_UU_12016/13NCI NIH HHS P30 CA013696NIGMS NIH HHS K99 GM134180NIGMS NIH HHS R35 GM118015Wellcome Trust 102943/Z/13/Z
6 · The paper itself

Abstract

Nucleosomes are disrupted transiently during eukaryotic transcription, yet the displaced histones must be retained and redeposited onto DNA, to preserve nucleosome density and associated histone modifications. Here, we show that the essential Spt5 processivity factor of RNA polymerase II (Pol II) plays a direct role in this process in budding yeast. Functional orthologues of eukaryotic Spt5 are present in archaea and bacteria, reflecting its universal role in RNA polymerase processivity. However, eukaryotic Spt5 is unique in having an acidic amino terminal tail (Spt5N) that is sandwiched between the downstream nucleosome and the upstream DNA that emerges from Pol II. We show that Spt5N contains a histone-binding motif that is required for viability in yeast cells and prevents loss of nucleosomal histones within actively transcribed regions. These findings indicate that eukaryotic Spt5 combines two essential activities, which together couple processive transcription to the efficient capture and re-deposition of nucleosomal histones.

Indexed as

ChromatinChromatin Assembly and DisassemblyChromosomal Proteins, Non-HistoneHistonesNucleosomesProtein BindingRNA Polymerase IISaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscriptional Elongation FactorsTranscription, GeneticChromatinChromosomal Proteins, Non-HistoneHistonesNucleosomesRNA Polymerase IISaccharomyces cerevisiae ProteinsSPT5 transcriptional elongation factorTranscriptional Elongation FactorschromatinhistoneRNA polymerase IISpt5transcription

Identifiers

PMID35102600
PMCPMC8886531
OpenAlexW4210613892

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.