Europe PMC

This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our privacy notice and cookie policy.

Structural Insights into the Association of Hif1 with Histones H2A-H2B Dimer and H3-H4 Tetramer.

Author information

Affiliations

  • 1. Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, People's Republic of China; Key Laboratory of Structural Biology, Chinese Academy of Sciences, Hefei, Anhui 230026, People's Republic of China.
      Authors
    • Zhang M 1
    • Liu H 1
    • Gao Y 1
    • Zhu Z 1
    • Zheng P 1
    • Xue L 1
    • Teng M 1
    • Niu L 1
    (8 authors)
  • 2. State Key Laboratory of Genetic Engineering and School of Life Sciences, Fudan University, Shanghai 200438, People's Republic of China.
      Authors
    • Chen Z 2
    • Li J 2
    (2 authors)

ORCIDs linked to this article

Structure (London, England : 1993), 08 Sep 2016, 24(10):1810-1820
https://doi.org/10.1016/j.str.2016.08.001 PMID: 27618665 

Abstract 

Histone chaperones are critical for guiding specific post-transcriptional modifications of histones, safeguarding the histone deposition (or disassociation) of nucleosome (dis)assembly, and regulating chromatin structures to change gene activities. HAT1-interacting factor 1 (Hif1) has been reported to be an H3-H4 chaperone and to be involved in telomeric silencing and nucleosome (dis)assembly. However, the structural basis for the interaction of Hif1 with histones remains unknown. Here, we report the complex structure of Hif1 binding to H2A-H2B for uncovering the chaperone specificities of Hif1 on binding to both the H2A-H2B dimer and the H3-H4 tetramer. Our findings reveal that Hif1 interacts with the H2A-H2B dimer and the H3-H4 tetramer via distinct mechanisms, suggesting that Hif1 is a pivotal scaffold on alternate binding of H2A-H2B and H3-H4. These specificities are conserved features of the Sim3-Hif1-NASP interrupted tetratricopeptide repeat proteins, which provide clues for investigating their potential roles in nucleosome (dis)assembly.

Full text links 

Read article at publisher's site: https://doi.org/10.1016/j.str.2016.08.001

Read article for free, from open access legal sources, via Unpaywall: http://www.cell.com/article/S0969212616302325/pdfUnpaywall

Citations & impact 

Impact metrics

10
Citations
Jump to Citations
8
Data citations
Jump to Data

Citations of article over time

Alternative metrics

Altmetric item for https://www.altmetric.com/details/11974175
Altmetric
Discover the attention surrounding your research
https://www.altmetric.com/details/11974175

Smart citations by scite.ai
Smart citations by scite.ai include citation statements extracted from the full text of the citing article. The number of the statements may be higher than the number of citations provided by EuropePMC if one paper cites another multiple times or lower if scite has not yet processed some of the citing articles.
Explore citation contexts and check if this article has been supported or disputed.
https://scite.ai/reports/10.1016/j.str.2016.08.001

Supporting
Mentioning
Contrasting
1
12
0

Article citations

Go to all (10) article citations

Data 

Similar Articles 

To arrive at the top five similar articles we use a word-weighted algorithm to compare words from the Title and Abstract of each citation.

Funding 

Funders who supported this work.

Ministry of Science and Technology of the People's Republic of China (4)

National Natural Science Foundation of China (2)