Structural basis for histone H3 recognition by NASP in ArabidopsisFA

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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.

作者 Yanhong Liu ^[1] Liu Chen ^[2] Na Wang ^[2] Baixing Wu ^[2] Hongyu Bao ^[2] Hongda Huang ^[2] 学术成果认领

作者单位 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 ^[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]

关键词 Arabidopsis NASP ASF1 crystal structure epi-genetics histone chaperone histone H3

栏目名称 Breakthrough Report

发布时间 2023-01-13

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