Evidence map›Paper›PMID 21757688›Full record

ArticleThe Journal of biological chemistry2011

The histone chaperone facilitates chromatin transcription (FACT) protein maintains normal replication fork rates.

Takuya Abe, Kazuto Sugimura, Yoshifumi Hosono, Yasunari Takami, Motomu Akita, Akari Yoshimura, Shusuke Tada, Tatsuo Nakayama, Hiromu Murofushi, Katsuzumi Okumura and 4 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

51 citing papers in PubMed, 85 citations in OpenAlex.

  1. Article
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  5. Review
  6. Article
  7. Beyond Chaperoning: The Multifaceted Role of FACT in Chromatin Transactions.International journal of molecular sciences · 2025
    Review
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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

14 authors at 7 institutions in 1 country.

Takuya AbeMolecular Cell Biology Laboratory, Graduate School of Pharmaceutical Sciences, Tohoku University, Miyagi 980-8578.
Kazuto SugimuraDepartment of Life Science, Graduate School of Bioresources, Mie University, Mie 514-8507; Department of Biochemistry and Proteomics, Graduate School of Medicine, Mie University, Mie 514-8507.
Yoshifumi HosonoMolecular Cell Biology Laboratory, Graduate School of Pharmaceutical Sciences, Tohoku University, Miyagi 980-8578.
Yasunari TakamiDepartment of Medical Sciences, Section of Biochemistry and Molecular Biology, Miyazaki Medical College, University of Miyazaki, Miyazaki 889-1692.
Motomu AkitaMolecular Cell Biology Laboratory, Graduate School of Pharmaceutical Sciences, Tohoku University, Miyagi 980-8578.
Akari YoshimuraMolecular Cell Biology Laboratory, Graduate School of Pharmaceutical Sciences, Tohoku University, Miyagi 980-8578; Research Institute of Pharmaceutical Sciences, Faculty of Pharmacy, Musashino University, Tokyo 202-8585.
Shusuke TadaMolecular Cell Biology Laboratory, Graduate School of Pharmaceutical Sciences, Tohoku University, Miyagi 980-8578.
Tatsuo NakayamaDepartment of Medical Sciences, Section of Biochemistry and Molecular Biology, Miyazaki Medical College, University of Miyazaki, Miyazaki 889-1692.
Hiromu MurofushiDepartment of Applied Molecular Biosciences, Graduate School of Medicine, Yamaguchi University, Yamaguchi 753-8512.
Katsuzumi OkumuraDepartment of Life Science, Graduate School of Bioresources, Mie University, Mie 514-8507.
Shunichi TakedaDepartment of Radiation Genetics, Faculty of Medicine, Kyoto University, Koyoto 606-8501.
Masami HorikoshiLaboratory of Developmental Biology, Institute of Molecular and Cellular Biosciences, The University of Tokyo, Tokyo 111-0032, Japan. Electronic address: horikosh@am.iu-tokyo.ac.jp.
Masayuki SekiMolecular Cell Biology Laboratory, Graduate School of Pharmaceutical Sciences, Tohoku University, Miyagi 980-8578. Electronic address: seki@mail.pharm.tohoku.ac.jp.
Takemi EnomotoMolecular Cell Biology Laboratory, Graduate School of Pharmaceutical Sciences, Tohoku University, Miyagi 980-8578; Research Institute of Pharmaceutical Sciences, Faculty of Pharmacy, Musashino University, Tokyo 202-8585. Electronic address: t_eno@musashino-u.ac.jp.
Tohoku University · JPMie University · JPUniversity of Miyazaki · JPKyoto University · JPMusashino University · JPThe University of Tokyo · JPYamaguchi University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ordered nucleosome disassembly and reassembly are required for eukaryotic DNA replication. The facilitates chromatin transcription (FACT) complex, a histone chaperone comprising Spt16 and SSRP1, is involved in DNA replication as well as transcription. FACT associates with the MCM helicase, which is involved in DNA replication initiation and elongation. Although the FACT-MCM complex is reported to regulate DNA replication initiation, its functional role in DNA replication elongation remains elusive. To elucidate the functional role of FACT in replication fork progression during DNA elongation in the cells, we generated and analyzed conditional SSRP1 gene knock-out chicken (Gallus gallus) DT40 cells. SSRP1-depleted cells ceased to grow and exhibited a delay in S-phase cell cycle progression, although SSRP1 depletion did not affect the level of chromatin-bound DNA polymerase α or nucleosome reassembly on daughter strands. The tracking length of newly synthesized DNA, but not origin firing, was reduced in SSRP1-depleted cells, suggesting that the S-phase cell cycle delay is mainly due to the inhibition of replication fork progression rather than to defects in the initiation of DNA replication in these cells. We discuss the mechanisms of how FACT promotes replication fork progression in the cells.

Indexed as

DNA ReplicationTranscription, GeneticAnimalsCell CycleChickensChromatinDNA-Binding ProteinsEpigenesis, GeneticFlow CytometryHigh Mobility Group ProteinsHistone ChaperonesHistonesHumansMolecular ChaperonesNucleosomesS PhaseChromatinDNA-Binding ProteinsHigh Mobility Group ProteinsHistone ChaperonesHistonesMolecular ChaperonesNucleosomesSSRP1 protein, humanTranscriptional Elongation Factors

Identifiers

PMID21757688
PMCPMC3162410
OpenAlexW2034714666

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.