| Literature DB >> 33199628 |
Qiang Luo1, Baihui Wang1, Zhen Wu1, Wen Jiang1, Yueyue Wang2, Kangxi Du1, Nana Zhou1, Lina Zheng2, Jianhua Gan3, Wen-Hui Shen1,4, Jinbiao Ma5, Aiwu Dong6.
Abstract
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 α-helix (αN) 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 αN, 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.Entities:
Keywords: H2A-H2B; NAP1 family protein; crystal structure
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Year: 2020 PMID： 33199628 PMCID： PMC7720177 DOI： 10.1073/pnas.2011089117
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205