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Publication Abstract from PubMed

Nucleosome Assembly Protein 1 (NAP1) family proteins are evolutionarily conserved histone chaperones that play important roles in diverse biological processes. In this study, we determined the crystal structure of Arabidopsis NAP1-Related Protein 1 (NRP1) complexed with H2A-H2B and uncovered a previously unknown interaction mechanism in histone chaperoning. Both in vitro binding and in vivo plant rescue assays proved that interaction mediated by the N-terminal alpha-helix (alphaN) domain is essential for NRP1 function. In addition, the C-terminal acidic domain (CTAD) of NRP1 binds to H2A-H2B through a conserved mode similar to other histone chaperones. We further extended previous knowledge of the NAP1-conserved earmuff domain by mapping the amino acids of NRP1 involved in association with H2A-H2B. Finally, we showed that H2A-H2B interactions mediated by alphaN, earmuff, and CTAD domains are all required for the effective chaperone activity of NRP1. Collectively, our results reveal multiple interaction modes of a NAP1 family histone chaperone and shed light on how histone chaperones shield H2A-H2B from nonspecific interaction with DNA.

NAP1-Related Protein 1 (NRP1) has multiple interaction modes for chaperoning histones H2A-H2B.,Luo Q, Wang B, Wu Z, Jiang W, Wang Y, Du K, Zhou N, Zheng L, Gan J, Shen WH, Ma J, Dong A Proc Natl Acad Sci U S A. 2020 Dec 1;117(48):30391-30399. doi: , 10.1073/pnas.2011089117. Epub 2020 Nov 16. PMID:33199628^[3]

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