Evidence map›Paper›PMID 26908650›Full record

ArticleNucleic acids research2016

A DNA binding winged helix domain in CAF-1 functions with PCNA to stabilize CAF-1 at replication forks.

Kuo Zhang, Yuan Gao, Jingjing Li, Rebecca Burgess, Junhong Han, Huanhuan Liang, Zhiguo Zhang, Yingfang Liu

Abstract read
In one paragraph

Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
–field-weighted citation impact
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

37 citing papers in PubMed.

  1. Review
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  3. Article
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  5. Review
  6. Article
  7. Article
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  9. Article
  10. Article
  11. Article
  12. Review
  13. The Histone Chaperone Network Is Highly Conserved inInternational journal of molecular sciences · 2023
    Article
  14. Review
  15. Unorthodox PCNA Binding by Chromatin Assembly Factor 1.International journal of molecular sciences · 2022
    Article
  16. Article
  17. CRL4Genes · 2022
    Review
  18. Article
  19. Article
  20. Article
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

8 authors.

Kuo ZhangState Key Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang District, Beijing 100101, China University of the Chinese Academy of Sciences, Beijing 100049, China.
Yuan GaoDepartment of Biochemistry and Molecular Biology, Mayo Clinic, Rochester, MN 55905, USA.
Jingjing LiState Key Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang District, Beijing 100101, China.
Rebecca BurgessDepartment of Biochemistry and Molecular Biology, Mayo Clinic, Rochester, MN 55905, USA.
Junhong HanState Key Laboratory of Biotherapy and Cancer Center, Division of Abdominal Cancer, West China Hospital, Sichuan University, and National Collaborative innovation Center for Biotherapy, Chengdu 610041, China.
Huanhuan LiangState Key Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang District, Beijing 100101, China.
Zhiguo ZhangDepartment of Biochemistry and Molecular Biology, Mayo Clinic, Rochester, MN 55905, USA zhang.zhiguo@mayo.edu.
Yingfang LiuState Key Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang District, Beijing 100101, China liuy@ibp.ac.cn.

Funding

Mechanisms of Epigenetic inheritanceR35GM118015 · NIGMS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI Zhiguo Zhang · 2016 to 2026
$9.5M
Histone chaperones and transcriptional silencingR01GM072719 · NIGMS · MAYO CLINIC ROCHESTER · PI ZHANG, ZHIGUO · 2005 to 2015
$2.9M
Regulation of Nucleosome AssemblyR01GM081838 · NIGMS · MAYO CLINIC ROCHESTER · PI ZHANG, ZHIGUO · 2008 to 2015
$2.4M
NIGMS NIH HHS R01 GM072719NIGMS NIH HHS R01 GM081838NIGMS NIH HHS R35 GM118015
6 · The paper itself

Abstract

Chromatin assembly factor 1 (CAF-1) is a histone H3-H4 chaperone that deposits newly synthesized histone (H3-H4)2 tetramers during replication-coupled nucleosome assembly. However, how CAF-1 functions in this process is not yet well understood. Here, we report the crystal structure of C terminus of Cac1 (Cac1C), a subunit of yeast CAF-1, and the function of this domain in stabilizing CAF-1 at replication forks. We show that Cac1C forms a winged helix domain (WHD) and binds DNA in a sequence-independent manner. Mutations in Cac1C that abolish DNA binding result in defects in transcriptional silencing and increased sensitivity to DNA damaging agents, and these defects are exacerbated when combined with Cac1 mutations deficient in PCNA binding. Similar phenotypes are observed for corresponding mutations in mouse CAF-1. These results reveal a mechanism conserved in eukaryotic cells whereby the ability of CAF-1 to bind DNA is important for its association with the DNA replication forks and subsequent nucleosome assembly.

Indexed as

DNA ReplicationProtein Interaction Domains and MotifsReplication OriginAnimalsChromatin Assembly Factor-1HistonesMiceModels, MolecularMutationNucleic Acid ConformationProliferating Cell Nuclear AntigenProtein BindingProtein ConformationRecombinant Fusion ProteinsStructure-Activity RelationshipChromatin Assembly Factor-1HistonesProliferating Cell Nuclear AntigenRecombinant Fusion Proteins

Identifiers

PMID26908650
PMCPMC4914081

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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.