J Integr Plant Biol. ›› 2022, Vol. 64 ›› Issue (12): 2309-2313.DOI: 10.1111/jipb.13277

• Breakthrough Report • Previous Articles     Next Articles

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:2022-05-19 Published:2022-12-01

Abstract:

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.

Editorial Office, Journal of Integrative Plant Biology, Institute of Botany, CAS
No. 20 Nanxincun, Xiangshan, Beijing 100093, China
Tel: +86 10 6283 6133 Fax: +86 10 8259 2636 E-mail: jipb@ibcas.ac.cn
Copyright © 2022 by the Institute of Botany, the Chinese Academy of Sciences
Online ISSN: 1744-7909 Print ISSN: 1672-9072 CN: 11-5067/Q
备案号:京ICP备16067583号-22