典型文献
Structural basis for histone H3 recognition by NASP in ArabidopsisFA
文献摘要：
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 nu-cleosome assembly activity in vitro. Examining the structure of AtNASP complexed with a his-tone 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.
文献关键词：
中图分类号：
作者姓名：
Yanhong Liu;Liu Chen;Na Wang;Baixing Wu;Hongyu Bao;Hongda Huang
作者机构：
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
文献出处：
引用格式：
[1]Yanhong Liu;Liu Chen;Na Wang;Baixing Wu;Hongyu Bao;Hongda Huang-.Structural basis for histone H3 recognition by NASP in ArabidopsisFA)[J].植物学报（英文版）,2022(12):2309-2313
A类：
ArabidopsisFA,autoantigenic,AtNASP,cleosome,SILENCING,ASF1
B类：
Structural,basis,histone,H3,recognition,by,structural,chaperone,nuclear,sperm,protein,remains,largely,unclear,Here,showed,that,thaliana,monomer,displays,robust,assembly,activity,vitro,Examining,structure,complexed,peptide,revealed,binding,mode,conserved,human,recognizes,terminal,region,distinct,from,Moreover,forms,ANTI,FUNCTION,Therefore,deciphered,interaction
AB值：
0.416762
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