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Publication Abstract from PubMed

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 alpha3 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.

Structural basis for histone H3 recognition by NASP in Arabidopsis.,Liu Y, Chen L, Wang N, Wu B, Bao H, Huang H J Integr Plant Biol. 2022 Dec;64(12):2309-2313. doi: 10.1111/jipb.13277. Epub , 2022 Jun 13. PMID:35587028^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.