Evidence map›Paper›PMID 28369616›Full record

ArticleNucleic acids research2017

NAP1L1 accelerates activation and decreases pausing to enhance nucleosome remodeling by CSB.

Ju Yeon Lee, Robert J Lake, Jaewon Kirk, Vilhelm A Bohr, Hua-Ying Fan, Sungchul Hohng

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2017. 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
1.8field-weighted citation impact, top 15% 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, 34 citations in OpenAlex.

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  8. A novelFrontiers in genetics · 2024
    Article
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  14. Review
  15. NAP1-Related Protein 1 (NRP1) has multiple interaction modes for chaperoning histones H2A-H2B.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  16. Article
  17. 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

6 authors at 3 institutions in 2 countries.

Ju Yeon LeeDepartment of Physics and Astronomy, Seoul National University, Seoul 08826, Republic of Korea.
Robert J LakeEpigenetics Institute, Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA.
Jaewon KirkDepartment of Physics and Astronomy, Seoul National University, Seoul 08826, Republic of Korea.
Vilhelm A BohrLaboratory of Molecular Gerontology, National Institute on Aging, National Institutes of Health, Baltimore, MD 21224, USA.
Hua-Ying FanEpigenetics Institute, Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA.
Sungchul HohngDepartment of Physics and Astronomy, Seoul National University, Seoul 08826, Republic of Korea.
Seoul National University · KRUniversity of Pennsylvania · USNational Institute on Aging · US

Funding

The role of the Cockayne syndrome proteinZIAAG000722 · NIA · NATIONAL INSTITUTE ON AGING · PI FERRUCCI, LUIGI · 2009 to 2023
$9.1M
Basis for genotoxic stress relief by ATP-dependent chromatin remodelersR01GM115888 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI FAN, HUA-YING · 2015 to 2018
$1.2M
NIGMS NIH HHS R01 GM115888
6 · The paper itself

Abstract

Cockayne syndrome protein B (CSB) belongs to the SWI2/SNF2 ATP-dependent chromatin remodeler family, and CSB is the only ATP-dependent chromatin remodeler essential for transcription-coupled nucleotide excision DNA repair. CSB alone remodels nucleosomes ∼10-fold slower than the ACF remodeling complex. Strikingly, NAP1-like histone chaperones interact with CSB and greatly enhance CSB-mediated chromatin remodeling. While chromatin remodeling by CSB and NAP1-like proteins is crucial for efficient transcription-coupled DNA repair, the mechanism by which NAP1-like proteins enhance chromatin remodeling by CSB remains unknown. Here we studied CSB's DNA-binding and nucleosome-remodeling activities at the single molecule level in real time. We also determined how the NAP1L1 chaperone modulates these activities. We found that CSB interacts with DNA in two principle ways: by simple binding and a more complex association that involves gross DNA distortion. Remarkably, NAP1L1 suppresses both these interactions. Additionally, we demonstrate that nucleosome remodeling by CSB consists of three distinct phases: activation, translocation and pausing, similar to ACF. Importantly, we found that NAP1L1 promotes CSB-mediated remodeling by accelerating both activation and translocation. Additionally, NAP1L1 increases CSB processivity by decreasing the pausing probability during translocation. Our study, therefore, uncovers the different steps of CSB-mediated chromatin remodeling that can be regulated by NAP1L1.

Indexed as

Transcription, GeneticAdenosine TriphosphateChromatinChromatin Assembly and DisassemblyDNA HelicasesDNA RepairDNA Repair EnzymesHistone ChaperonesHumansNucleosome Assembly Protein 1NucleosomesPoly-ADP-Ribose Binding ProteinsAdenosine TriphosphateChromatinDNA HelicasesDNA Repair EnzymesERCC6 protein, humanHistone ChaperonesNAP1L1 protein, humanNucleosome Assembly Protein 1NucleosomesPoly-ADP-Ribose Binding Proteins

Identifiers

PMID28369616
PMCPMC5416873
OpenAlexW2603371662

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.