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 n...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 H3α3 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.展开更多
基金the National Key R&D Program of China(2018YFC1004500)the Natural Science Foundation of Guangdong Province(2022A1515010501)+4 种基金the Chinese National Natural Science Foundation(32171206 and 31800619)the Shenzhen Science and Technology Program(KQTD20190929173906742)Key Laboratory of Molecular Design for Plant Cel Factory of Guangdong Higher Education Institutes(2019KSYS006)the Shenzhen Government‘Peacock Plan’(Y01226136)the Thousand Young Talents Program。
文摘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 H3α3 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.
