拟南芥中 NASP 识别组蛋白 H3 的结构基础。

Structural basis for histone H3 recognition by NASP in Arabidopsis.

机构信息

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.

School of Life Science and Technology, Harbin Institute of Technology, Harbin, 150080, China.

出版信息

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

DOI:10.1111/jipb.13277

PMID:35587028

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.

摘要

组蛋白伴侣核自身抗原性精子蛋白（NASP）识别组蛋白的结构基础在很大程度上仍不清楚。在这里，我们表明拟南芥 AtNASP 是一个单体，并在体外显示出强大的核小体组装活性。研究 AtNASP 与组蛋白 H3α3 肽复合物的结构揭示了一种在人类 NASP 中保守的结合模式。AtNASP 识别 H3 N 端区域不同于人类 NASP。此外，AtNASP 通过与 H3 N 端区域结合与反沉默功能 1（ASF1）形成共伴侣复合物。因此，我们破译了 AtNASP 的结构及其与 H3 相互作用的基础。