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. 2022 Dec;64(12):2309-2313.
doi: 10.1111/jipb.13277. Epub 2022 Jun 13.

Structural basis for histone H3 recognition by NASP in Arabidopsis

Yanhong Liu  1   2 , Liu Chen  1 , Na Wang  1 , Baixing Wu  1 , Hongyu Bao  1 , Hongda Huang  1
Affiliations

Structural basis for histone H3 recognition by NASP in Arabidopsis

Yanhong Liu et al. J Integr Plant Biol. 2022 Dec.

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.

Keywords: ASF1; Arabidopsis NASP; crystal structure; epigenetics; histone H3; histone chaperone.

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