J Integr Plant Biol.

• Breakthrough Report •    

Structural basis for histone H3 recognition by NASP in Arabidopsis

Yanhong Liu1,2, Liu Chen1, Na Wang1, Baixing Wu1, Hongyu Bao1* and Hongda Huang1*   

  1. 1 Key Laboratory of Molecular Design for Plant Cell Factory of Guangdong Higher Education Institutes, Department of Biology, School of Life Sciences, Southern University of Science and Technology, Shenzhen 518055, China
    2 School of Life Science and Technology, Harbin Institute of Technology, Harbin 150080, China

    * Correspondences: Hongda Huang ((huanghd@sustech.edu.cn, Dr. Huang is responsible for the distribution of the materials associated with this article); Hongyu Bao (baohy@sustech.edu.cn)
  • Received:2022-02-15 Accepted:2022-05-12 Online:2022-06-13


The structural basis for histone recognition by the histone chaperone nuclear autoantigenic sperm protein (NASP) remains largely unclear. Here, we showed that Arabidopsis thaliana AtNASP is a monomer and displays robust nucleosome assembly activity in vitro. Examining the structure of AtNASP complexed with a histone H3 α3 peptide revealed a binding mode that is conserved in human NASP. AtNASP recognizes the H3 N-terminal region distinct from human NASP. Moreover, AtNASP forms a co-chaperone complex with ANTI-SILENCING FUNCTION 1 (ASF1) by binding to the H3 N-terminal region. Therefore, we deciphered the structure of AtNASP and the basis of the AtNASP–H3 interaction.

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