7C7X

Structural insights into nucleosome reorganization by NAP1-RELATED PROTEIN 1 (NRP1)

Summary for 7C7X

• Entry DOI: 10.2210/pdb7c7x/pdb
• Descriptor: Histone H2A.6, Histone H2B.1, NAP1-related protein 1, ... (5 entities in total)
• Functional Keywords: complex, histone, plant protein, chaperone, transcription-chaperone complex, transcription/chaperone
• Biological source: Arabidopsis thaliana (Mouse-ear cress); More
• Total number of polymer chains: 6
• Total formula weight: 97472.70

Authors

Luo, Q.,Baihui, W. (deposition date: 2020-05-27, release date: 2020-11-11, Last modification date: 2023-11-29)

Primary citation

Luo, Q.,Wang, B.,Wu, Z.,Jiang, W.,Wang, Y.,Du, K.,Zhou, N.,Zheng, L.,Gan, J.,Shen, W.H.,Ma, J.,Dong, A.
NAP1-Related Protein 1 (NRP1) has multiple interaction modes for chaperoning histones H2A-H2B.
Proc.Natl.Acad.Sci.USA, 117:30391-30399, 2020

PubMed 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 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.

PubMed: 33199628
DOI: 10.1073/pnas.2011089117

Experimental method

X-RAY DIFFRACTION (3 Å)