Structural basis for histone H3 recognition by NASP in Arabidopsis

被引：0

作者：

Yanhong Liu ^{[1
,2
]}

Liu Chen ^{[1
]}

Na Wang ^{[1
]}

Baixing Wu ^{[1
]}

Hongyu Bao ^{[1
]}

Hongda Huang ^{[1
]}

机构：

[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

[2] School of Life Science and Technology, Harbin Institute of Technology

来源：

JournalofIntegrativePlantBiology | 2022年 / 64卷 / 12期

关键词：

D O I：

暂无

中图分类号：

Q943.2 [植物基因工程];

学科分类号：

071007 ; 090102 ;

摘要：

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 Nterminal region.Therefore,we deciphered the structure of AtNASP and the basis of the AtNASP-H3 interaction.

引用

页码：2309 / 2313

页数：5

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